 

  

 

.0 . .... v .1 I . ii... I.
. .. 3..-7.300 ...-o. ..m

......hgwﬁw “in... .... .

I .. 000

 

      

     

              

         

. 0'. 0a ..0. .. 00..

.... ... ...... .... 0..
000.0. 0... I

o. ‘4 .00 . 0

              

       
              

_ m. ...: a... ..n a...
.uqsm. . .. was.-...u ......I..~......."
.. 0’ ’ . I :0.-!‘ 0—? 0.6. oL'“0noﬁhﬂ-§.¢O.f..n
. “u. L . . .Q000.;.“06M .sn%...d.m.0. 0.40
0 0‘.“ 0.4.0.40 .0. . 40.“...u10. '0.u0u..n.. n".
O. .00 .V l 0. . 0 0.2““... “w"..b‘oﬁoof:
.4... "may... 4.1225“... ..."...h........
..u «5’?- 10010. . .00.“ I 0.0.”

   

0 a ‘0
C 3.2.:

”....
.0

   

   

.—,. o
. q o . 0 . . . .
.. 0. . .. .... .L....o.1—....u:.ﬂ.o ..
.0 00.01. .I... 0.. 1.. 00...!0.uon.} 0.0.0

......1.3 ......x..§.-...
O A o . ..0

    

  

  
    

   

       

 

. ......ﬂ: Haﬁz;
2?...
0.: w #3....
..., .. N. . ,

.W .u0.0.~0 AA... .—.

  
  
   

    

   

 

00....- AH» -...0 .. .5 .c. o ..0. 0 '

. , are? ...u.
. ... 3..-u. .

    

    
   

      
  

  

 

. 30 5
.4: . 0,-1.0

      

    

   

         

       
  

               

      

   

          

               

    

 

   

001.
.. 5.00.. 0I J .
. 0“. “.0 €004,300“
3.7. . .0. '1 . A. 0 . -. O on ...”..0. . .. . 00.. 0. .... 0. 8 £33.... «0. 0 ...JW...’ 0
3 3700.0’0000..-” I0...) ... I . _ 0. .03 . “‘JdOr: .. 0
.... ... -. v I . ... .I .. I ...< ...gn.~0.b .
. . I. . .. .L . . o I... ... . IV I. . . a I .0: .I . o . 1.0.. .4 <
0.. I. 001! o 0.. . ......0: .0. 0....I ...0v4. 0 f; t .0 .... k”
...!I. .. 0 0‘: PL. . ..v .. .31.... 0. .... .0 .... . .3 0 I .
. 0. O. 0 .. I. o .0 .. v I Q . . I . . . . . . .
r 0 . .ou‘and 00.0 n. .0000. .0000. . .u ”.03!" 00. .’0 r “500””. 3"” .... 0. 3,1 4.0 ”0.. 0 .‘04? ..I o g a
. . I 0. ... .0 .00 . .. 1 . ...f . . :0, 0 3.90510 0 .0 ...0 0. “a“: ...-I I .0 I. 0 do
. .. . ... .. .._ 0 .. t .0. . . . ... .01
. .9 .... .30 , . . . .. .... 0. 00..
so. .00 0.4.003”? 0.000.0'0... I , I .0": .J . Pu .000 . ...... .
00.0“) . ... 00... .300” .0.‘00.00..
. ....“.00..0.0 ..

. a .0! 60
.I‘ v 50‘ 00.00 H.

. '2 {Canal-0.0.! ...0._ .:
.0000. . . o. .05.: ...... v
0“.m. o ...J 2.50:10‘ ...

  

. {.. 00 a . ..,. 7. «.....(I) “.53.
o 301...”..“01 “.0308 ......mw-Mh 30.... "0.33.00...- R’MHWM‘FMSIMW .0... J 330.... . WW“... L.
.v C .00.". 0.”OI.I.I .u .u...‘ 03HH000‘"..B: .01.
0.0.5,“ ....«u. ‘5‘”. .0. v. ”ﬁrhniﬂpﬁéax. 00.. "a.“ . .
.a. ..., .4 ....”h. ...... ..ﬂ........1w«a: ...
0. £05 ...I yk‘ :30. .2.) . .

.30. 7‘“. ....”50“. [$0 0.
3. .. .4... a. . ...... ...r .
.5 ‘0..- 0.I~0 I... .

o
. 0 .... .0. a .00 . .0. .
... 076.... .......v V... I. . ......“ffﬁﬁuw $6.8 w. u. .4 :1 0 .3 . a. .
a. ...I .0..1.o I‘. .. 0... . ......J ..01. .03....0300 . ...-1.00.5.0 .0 5'“

                

      

    

o I’00
. ... Daft: ..-. 0..

’17... 0.0. r if a. 2.... .
.....Z- ...... . ...0 «7.. ..0!.o...
. . .u’..0..:-00.~.u\w.0.40.0030.“! .0! ola-aﬂﬂﬂ 0.00 H0. .0. 0‘. id“ .0 n.-"”- 0.- 000 . 0.

       

 

                

...“...Z; "MM/36... ..u 0 ...-u.

   

   

     
       

   

    
   

 

      

0.
. ... . . ... I. ....f 0.. ...: . .

. . . w 0 . . I 0 . c .4 - . . u .5 .
0 . , . u“ .m.‘ .00 0 I. .w .. 0 ﬂ. _. an ..00 .p 4.1". .n. .0 ...“.00 0003:: 00....”m Goo..- 0.".‘u3 06.0 I.“
.. ... . .. . . . . on .. . .90. . . . 3
.... ... ...... ...}..“unrzu . .4“. .. . . . .. _. _ _ any...“ .... .0 .. _ .23.”... -........“...ﬂu.....nau...¥d.. ... ....
00300.30. *IV00... 6.0 0 ......0. . $0: .4. .. 0.! ~00, . 0... [.00. ...-Jr .0... 0.3 .0... .0! .0 .. a 0 0d

00.0 . .. .. 0.0.0."..- s ...... .0. 0 I“ 0. 0?... .0000... . . a. . 0- .. 0. .00.. .

. ...‘...‘O...0.33.0 ...... ... ,.. a

 

 

.v 0... . -0 I ......20
...... a . -......
.. .01.! 0. ..0 i... n. o. . a 0 o
000-. 0.!......a."-...1r..~‘00.0 s P . .. .30 .. l........ .
. 0:. 0., 00. 0...... $0.00!? 0..
.. .0..I_.¢_. 0.0 ‘;|

. s. ....I'..0. a . . .. . 00
......u...«”.3.0 [00.0 I . 1.....ﬂn...pnnbhkmhuorlo.‘ ... 0.‘oom.~0h.
........ 3... . r...2..ﬁ....,.... 5..."... an...
1.. ... .010..La o... t“... .0.. 2,. ”M
... 0.. 0 ....Dv.0-00 0.3.0.70
0 . .04.“ ‘4 00 0. 5.0.2..
. .0 . .0 04 .0 .. 0.0
. ‘ «do 1000.! .0. . ”0. 0h"
'3 . .. )0 ...

....uuﬁwv

          

 

  

. a...
3 .0; 0.0 .... .I
a.

 

.04.0(0t..ﬂl.b. .p .u ... 0.
an...

       
    

           

 

     

        

   

            

  

           

 

 

      
          

         

        

    

   

    

 

..
.. . ... a. I , .....zxn ...... :2 .rn: 3...:
v . . I IO.I
.. . . .. 5.... ...... .. ... ... . . ... .... _ .... .... ....2....".._it. 1...... 3.... 3.»..1...2...i.
. 00. 00 0.00.07.03.90: 0:10 0 0. 50.. 0 u . ..0 . mun..v...v.w .0” .. . 0 -. .... 0.. 0 4 J. 0. o. 0”... 0.0. I \Io.\~.....b.. ... 0....09'oulauu. 3‘ I 2.0%.}.
. . .. . ., . I . . . . . I 0
03.....aJJ». . .310. ..J ...00...L..m ... ... . 0.. . . ... .L ....0. 30.32... . 2.2.915“... . 4. ......L...tv. 70.... A. ...UI‘...O. 0.4.03. til. 03 a. "I. .“Jmi
. . . l . . 0 .. . .I u. ._ 0 I. . 00 I . .4 .103...‘ ‘0

.00 .0 . ... . 0 ... 03¢. . . .... . . z.. . I .00... 0. 0 0 0 . 0 . n . 0.. . .

0. 30.00.... 10.53.00. . .0. 3100.70» .. ... ...-.0... ... 0% .....I .m‘ .0 v 0....1. . 1.. 0 .... ; o 0. I .... \.. . . 0 00H..-unm.l.0m ..nu.».‘r.70
ifi . ...-....PloNH0Q0Wrumn“;20!. 0 _ .0. 08‘ 01.. .... 0. .. .... .. IX.Io. ... f .70. 0 ......cc.... . ... . a.(‘. 0 . . o 0 0 . 0‘. . . n .00. (w .‘P‘
.. .nﬁgsw‘JuhUuquIs Pas. .6. It . .. 1.1 . . . u . . . .0 I o . I. an m......«....o....:.. ...... ....u. .00 .I .2~.~0€...W0.3.0

. o. . . ... I . . .. . I , _ .. .... . .0: :0: .3 .

. . .. . . . . . . ..03.V¢ .00 0. . . v . .. 00.40- ...

. ......n .. . ......su..." «. .. _ . . . ., . . _ . I , . . .. .. ﬁn... ...: 9.2.... Liar”... .. «.... _._ a. 2 .r.

0.1.0.00 . .. ..0 .. ...... 10.05.00.200... . 0.1.... I... I. .l ... I... .. .. , .....0. 4.0 .000» .v. I 0... . 00..DI.«1I. . ...‘0ﬂ00'l‘3o0r3’0 0 .I.0.0¢0
. 1.0.0. 5‘. I. .. . 0 .0. . ..0_. .. . .. . . . 00 I0 . .0! I . . . . 000 .
. ......Q 0.. . Joy... u .00.... 0. 3 u s . . .. 0 . . . . . ...... . 02:0” . 7.r v'P0 . ...... 3.0.... .3 «0‘03... .. 0 . I 10.00.00... . 1?”. .0 0
00.. ‘0 ...... . 0 ..H......_ ... .0. ..000. 0'00
9.4 0 0 o 0 . .‘ .0. ”0:. .J I“... v.0 H I 0. ...0 . a. ’0 0. I u .0
.I a. . .
0 05.10.

             

 

 

 

0:00 .0... ... . “
a}... .. n:....2......ﬁ.+........ad..u.n........:.....u. ..
. 0. ynl.0..0m000n.. 030.400.“. .0010 0.0 £000»; .0. I 10“..” ”c.

.. . . .I .. . I I
.. .-.... 5.44.1.3“... rho..rrot".r...,.n ...mnunuuga. ...

. 0. I. 0 .00 .0 0.}: . .
.00 0 I. .-.0‘,..§5: 0 0 0 .' I
......m...“ .3753.“......I........I....u...u._ ......nﬁﬁn In.

.. 6. . .0 .. ......0 co .
...... HF... ..................:................. ..s...w..a...uu..m.c.
. Q. .3...0.~$I.Aal 0. a... ’33. I .6..2.¢ 0-.

. .. I.
. ... . - .... 2:... . ...00 .
.-

...-10.09....3-
...-1 0. 0,.

 

.OJ0.1.0I.*“00. . 0 .. 0.00‘ l.

        

. RS“ ..
..0 0 . ......

        

0.0 . \ 0
0 9......3l
coo .... 00.0 .
.o .

0.

 

1 n
.0. 0 0'0 . ...l
Li? . . . I .

 

                   

 

    

l0 . ..-

 

   

        

  

     

        

 

   

     

 

    

              

 

            

 

       
  

        
      

  

 

           
      
    

          

  

 

   

 

      

 

 
 

            
             

   

      
   

  

    

 
  

. . .0 ’. ‘0 0L" 50.0
00. .0 .. q . . 0 .41. ..65 J0 00.... Q0) 10.0 03.1 1.0?
.9. ‘0. 0 ‘ ’30
. . ‘I .0000. 4 .. . 0.. ....o .. .t. 0... .... .0’3..I¢,..I\l...£.o§ .0!-
. . 0 ..0; “000.40 00 .4 . o .400. .0 I I.- Ino . v. 0 00.. . on]. u.....M0.v~n.vA...0. I0...l0...0 0.... ..00 0000”, I0m...’..
. ....c . .. .. 0.0.00.0 0. 0.5 0. a 00 0. 0 0 . 0. . I (0 0 '0 l I . . . ... 0. 0: .. 0 .0 . . .. . 10 0 ._ 00 00.03w0. 0\ {‘0 ‘00
- 05.“. v. . .00 00......" I.NN 0 01 VuIlbouoo. I. .I. 0. A . ..o 0... ..v2 00. .0 I c... 0 o ....a ..00 ...Iﬂtnf ..M.:“.0.v0.r.. 0.3th Mv 004”“..‘00'0. q .00 .Q 0.0 01"“.
.4 ~ . . . . 1 I . .. ... II. .00-.. .4. 0 0...!0 0‘ 0 . I . I 0 . I»! . v 5 13.0.0.0.0 .0 0.00‘0n'. 00~
...... ......r....r. . . ...... .... .... .. I . : I . . . . . .....:...................7 i
I... ...I. ... . . I . .u. . . .. . .. I. 0 . . ... . ... ...? I. . . . I... o I ,. .... .. 1 o . . . ... Eunihnw ...§53.3 ..
.. .. .. . . .... ... .. .I.. .. .. e : .....I. h... , 2-.....» .. ... ......:. -............... ._ ......J..._...r.u....£ 2......3321
. ... ... . . . . . . . I .. .. . .. .. .. 1 . .. . .963... . . v 0 210...?10 0.
.0 . h 0 ..1 . 0.0”“..3. _.IOIQ .u ..0 . 0 0‘IO.. . . 0...: .4“0 ML. 0 "‘J‘II” .00.. ”root0t0-sr o“... 00’0l0 IOIL.I....Q . . ,“0Ivouh-000u.k0“."ndhnywnu.“mul.mqnlt$tl ‘.000$
. . . u. v 0 ’00.... ' 0o . 0 _. i .42 o 0 . I 0. . . ... 0100 c . .I. 0‘ . .0 0 I . . 04.00.». .....‘olmdn ... O: . \I 0.0..‘00 ‘ 0
3.0.1....0 II .000 . 0 v. .0 . q . 0 A. 00 I. 00 .. .- . 0. n. .. . 0.1!.-.0. .09. I ou‘I‘00 . a .0011. . 0000 V a. at: ...—1..
. ... . 0. . 0 .220 . . 0... 0 ... '01:... . .0 . 0... i. u 0 . 0. § '00 ‘10. 0 0... '0 0.0 . 0.0 ..‘uz‘VI .ztuu‘c‘ﬂv ’00‘0‘3‘ .0 ....- I10
.... . ... . .. o .. . . . I \- ...... .. . .0 .3 . ... .. 7...... .p . 01.... ... 3303...: .......?~.0... w... n.8h3...0wauo . .3”... ‘ .
.. to... I . . . ...: .. . . . .. 0 .. 030 . .. 0 . I u . . . . . .. J 7‘ ...0 a I I .0. 0.0.. an. ‘00.
, on e .0 . I. . o 2 Ono . . . .d0... . I. ...; .0u.anbu ... , . ‘ .I1.u.00..0«h..00.......3«ﬂ.r.p.m.r.00”“..“01-4 .000.”
0 .l . . . 0 I 00.00. 0.0 ..I. o . .I‘ . o . . . ("‘00. 3..-5’60 .1 .0! {3.. . . I
.Il00 . .0 .003 I o o 0.. 0 o . .. . 000. 000.00 .I I. 0 - . J .30 0.7 -
O. 9’. .. .0 0:. .0 . 0 c 0 0 d 0. .. .00 00 0.0 “.0... “.... I. ":0 00....0-. . . .5... .00. .0 O (1.0 In“. ”0”"«uhwuu0.uhnfuo.h””§‘0000 ‘0‘. O . . ’llxl¢ d
I o 5 .u 0. .. ... . . 0 0-f... .. .l 000M0 .0 a . . .0300- .0 01‘.UOI.O: 0010’? ... unv‘runlzp." 0) (“‘0 “0 . _‘00 A ,I
a. c . no . ”0.... I. . . ...”. .... .0 0 n0. . .. 0.. . 01 .w. . 0!..0 .. . . . 30020.0 "Quid“: 5100.001?! 0.09%.. 0,0003: ar-ruao—Igrilﬂu0rh. I00. 0:, ll .ﬁm ﬂ
. ..u a . 0 . 0 £00 \ . . II . .H.. . . . . I... I0 0. . n . H ...... )4. 0-,.6 .10 ’0 00:00 ’4 ’ ..O n no . . , 0.
.. .0 0. . .... I. . . . v . . ...: .. .. .p ... ... ... ... .o 4... . . 10.. 0. . . . ...I: . . ..103 .. . ... .3- ..“u . .... 0 3.0-. if... .0. 014... i. . £030 '0 . “I“... 00. . 001 o J V. .... t 00.
. 00.....‘00.Mo..0d q . . . . . . L .. . .. . .. . . . . . .. . 2:... .0 ...c... .. ... I70.. I . I 0 . .0 . .. ... ......00. "09.0 . . o . 0... 00”.. Q. 31001.40. .0‘00 0 §._ .000. 0....‘lv...!. .F‘n¢.nup.p.unuhz.n...0‘b . .F 00.: 0'0 . .001“; G 0.." “m . 'u‘ §
...: . n. V. “I. 0. , . . . . . . .. . . . . . . . . . . .... I O. .0. .. . . I 3 . . 0,-0.0“? I. . . . . o . .04 u”. ..uIL... n. .00. “li0u4..00 .1... 0.0.. 0 ....0. 00.8%..J..00.”-0A0.“p0'0".00dn .0: .J. ... I00?” 3..": III 7 km HS ...“
. . . .. . . . ... , . . . . . . u .00 - .... . . o. . I .. ..o .. I. o . . . . . v 0 .0 .. .o . .. . . . . . .
. ...» .... . . . . ... . :2 .. .. . .. ...h . _ _ . 5.... ...... ...... ,- z .. .... .-....n....: 99.3.98...“ . .25.... ...ﬁﬁummu ...... {.8123 _
..I01... . “.... .. .v .4 I.... .. . ...: .n. .I I In” .. . 3...... . 0. O. H . ..HIQ. 0.. ' I f . . .036... 3' I. .-.." «00 Jinn-”.0J.,..nro 0 o. 33%..” ' Lyifufis ﬁ .0 ’4 2
_ . J0. ’60.) 0 I- o .. 0.. I a ; 0 .0 0 . 0.. . .0 .I 0 .. 40 0 . . ... 00“) 4.000 0 . ...:0 ‘0 0.0.04 .0 00 .0 _. a, . . l. 19.50: . .
7 I . . . ....Q . .... . .. . .. . ..I.. I. ...0 .. I .. 00-0 A. . o. . . . _ . . . ..0. . a Q 0., 0 0. 0 . 00.00.800.03 ‘1 r .0: v 0.!- a. z”
.. .. . .0 f ... . o .- 0 n0 3... . 0. II 3.00. . I .. ...0 . I3. . .I . . 1 . .. 40.0 I. . I»: . , . . C. . "00V0 10. ‘0 <0 0.... . 0.0000,}: (O... .chd :0. 4’7”“
_ _ ... L . ....JI} . ... 03.. . . ... fl .. . o . . . ..0. 0 I .. . . .I I . 0 .. .3 .. .10 .\ I. .. . . ...-u. . y I 0.. ..r.o..20..1.o.:‘o05. 0.0.3.”.030»! “II. 0
.0 0. . 0;...3... . I . . ......70. l . . c. I. .. 0 u. .. I . .0JP . '0 .I I 0 . 0 0 l . 0 .. . . . . 0. .I. 000A. .... '. ....- Ip‘ub 4......"00... b, .5 ‘1'
. . . . . . . . I . I . . . . . ..1’10 . 0‘. J] 0
. _a v. ... . .. . .. ... . . .. o .... I... .I I I. . ... . .I .. .. ...; I . o .1 . . . .. n . .. I . o .0. 0... . . .... h .0. .1: .0 a 00230-3100 11.201 3..-1.030300. J
3..... 3 "nib“.mt... u! . . .. I . ... .7- . . v 0 ..w. .. . . Hz}: . .0....L..l.... ....0 u. . 3 ....» n. I J ..Py, . .....v...H «P. I. .... 241:4 .dtuw-uhﬂﬁuoo.‘ ......v . .91.. ...-01.0. it: glut”...
a . . . . .. . . . .. .. 0 I . . x 0 0 .0 o . . or . so..I-0 O. . I. I: . 0 .. 0 ..0 ‘0 000.. .... .
I ... .0 . Haw-30.. .1 _ . 0.0.". ....I . .c . 1...... 0 .. p . . . "1.0 b . .. I o ”v.0... 00. .... . . 0. . 0... I . . .I o ...‘0. I”... . ..I0h . .0. .'0..su' 4‘; -
v00. 0 .p . z 0.. .o 0. . . I . . . .. . . . .. . . 00. . . 0 . .. .0 . .. ' 0 .0.0 .... s. u... ... . 1. I r . o 00 .0. n ...I 7 3.0‘40 00 I
. ... . . . .40. .. 0 I . 0 ..0 .0 I0 ‘0 1. 0 .I I 0 h 0 30¢ .... 0 I. 00. 0 .0. ...-0. I. .. .I. \. 0050...: . a‘d‘ v).
. . _. - ... ...- ... .. . . . . .n . .....L. - ...... ... -. .. .. - ., -.-. ... . ... ... . .. I 3. .... ..2. .. ...i ......
...q.. .. .0... .I I. 7.. .... . . 0. 30 . ..9 . . 0- .. .0... . ...I: . . ...t. 01. r..04...0.l
I 0. . ... o . o b .4 . \ 0 .o O. 0 . . 2 . 0:. . 0 00 I... .- ... . I... 0 .0. 0 . . 0 0.0.0 0 . I. 0 00 ‘5‘,
I- I 3th . u .. . . . .. I. I 0.. o. . ..LII 0.. 0. I. u 00“.... ... 0 0. . . 2 . .30. .l ... I. o 00 0 0.: . . . . OI . 0 I 0 0 VI . a. ... 0.. _ I ‘0 0
. .. 0 . s. .0. . ...II . I .. ﬂ.” 0. 0 . 0.. . . I 0. . . 0 I Q 7... .0.. 0 O .00 ur00u..l .‘..00 0- I 0 ... ‘u00ou. 0 0.00 I 0.004 (”.0 0 ' 0.0 .‘ O", u ‘4. .0” (0 '00 ’0 00
I . . I I I . u . 0 Q. ... .. .‘ooo..-0 . 0- ... .004
. I . .... .. . .. I c 0. . . I . I . . I ..I\ o 0 0. . . A. 0 4 0. 0. I . I ..v. o. 0 . .I . .....f? . . .. . .0 0 $.30 00 .
~01 “1.3.00. .v. .. s ..0 0.. .0. .0 .0. . . . . 00 ‘0‘. . O I I..\I.O .0 .. V. r .o .I .. ..‘2 . . ... . 0.. 3 0 0-H“; .0.- IY. ...-020.?”‘0 '0 .0.
a ._ . . . . 0 I . In. I A v - 4.0 . o 0 0'. ..I v 0 ...! .. 0 ‘0. s. A I I I u 0 .... p .. . I 0 I I .0 000 , A 4 .00 .I . 0'4
. .... I . . .. . .. 0 . .. . . . . . . . 0. . .... . ...... 2.... ...; Ii... . ..V.. . Ii...
.. .‘ ... 0. .I\ 0 . o . .Q.. . I 0 00 0 I . O .... ......Il . ..I I . . .... 0..., ...- . (a... 0.0 0.... 10.0.03910.
...h o. _. s .0 c . .0 I I 0 '- . ~ . o . I . a. 0 0 I .n .0. . ..I 00' ”00 3 u 0 . 0.0 0.. c 0 . . . o. .3 . 0 . ...o, .o .o 60.0). .‘\o ' ‘ I ‘2 . .0 ‘0’)..910
... . o.‘ v I I ... o .I I A. J 0. 0 .. a .0 a . ... p . ....-. 0 O b. .00 . . ..I 0 0. Q. 0. ...“: 0...:-
O . ~ . 0: o 0.. . I. . . .. . .0 0 . I. I 4 0 .II 00. . . . g 00 0 00 I I. . 0 .. .0 00.6 . 0 0:01. .0: V
I I... 1'00 . 4 .0 . 0 . . o c 0 I... I \ H .0 0 o v 0 .uﬁio: 0 . s 0 o r I . 0.VI . . :00. .000 . a. .
n . .. . .... . I I o v l .. I o I O. o I. n I. . .. . 1.0.00
... o 0 (IA... 0.. ‘0 CI 00 J. o 6.0 .... 0.9. o a. o 00. t 0- I .0.0 . .0 .0... .00 .o u . 0.0 .. . I.I-"0J .0 1. 0n0 l
, . . . l . . . I .c . u . I l . ... I. . 00 . . I . 0. \ 0 u 0 .
«I... . I. . . ... . .0... .0 O 0. ...... - . . . o 0 .0. .. .. ....0 I." ..n- ... . 0 . 00.. .. . . u. a...- n o 4 . . t 0. .m .o .u \C‘u..0.£s .
. 0 I . . I . u I . a n . . u . n. I 0 a I 0 0 . . . I .I . . I . . . ii
0.... I 4 . I I. .I. 5.. . a . . . 0 I .r o. . 0. ...; I0 . . . . .... ..0. . 0 .. I . I . .. . . . v. . . . 4.070 I . . _.0 4.4.03.0: . ..
. _ ... I, 5 . ... . 0. n . 0.0. 0 . I 0 . 0. . 0 0 000.0 0. n. . 1 300 u 00. '...'.l000v0‘03 L1 .
. . . . . . ... . . . . I o .. .I .. .. . ... 0. .0 ... 4. .I . .. I . . . . . . . . .. ... I. . . ..50 0.00.0.- ...£0. . , . .. do‘f ...... IN. . 6 1.0.
...H .7. ... _. . . .. .. I . . . ..- . . 0 .. 0. n .2 .....i _. . . 0. . .0 I . 0 r... . .I: I .... .. . .- .03 ... .. . 0. . 6.211003“ 0.00.... 4 lick
._ . . I .. . .... . II . . . .II .. .. . _ . I . o ..10‘ . .
. . _. . H. __N ..... . . I. .. I. . . . (I . . :0 O. 0 . ... .. .i I. ... IV 0 0 ... .....I . 0.9. .h. 00. I3... 1. . A . ....0 “”334.""...“...vranvHu (“03"...0030.) .Wscb‘u....”’..” Ham-00.100... ‘9. ’15.. £000.
. .... .. .. .r _. - . . _ . . . . . . - -.. ... I. . .. - .2. .. . _ : ... .. . - . .... . _ _ Lu... .... . ......n.....?.. .... ...... .43. ......Iiuésnanhx... .2252... {2%. 3.2.3
_ . . . 1...: 3 I . . . - ... . I ...: . -I ... ..0. ... .... . . , . ,. .-. . . _ . ...... . .. ...... .....- ......t. . 1 . . . .. 38.003. .0.
. I... . ... I 0.. 0 .0... ... .. . .. . I 0 .. I I . . 0. I . .0. In”. .. 4. .. ... . . 0 .I I ...0.. O .. - . I I .0 ul- L. . .. . O .0 - . .50. I...‘.Q....n.0! w. 3.0... “qﬂ’u’owgonfol . 03,0 30:,0‘ a“
as .V . . . . . a . . .0 o 0 o . I . ... ... ..N . ... .0 . I a. J . 5 . . . ... _. VI. .00 “I”. .... ‘ 0... .04).... 0s. J ’. I. ..00.00. 300p 0 0. ‘ ’2“....ﬂ.00_l.‘bﬁ .0... I.“ .
... . . _ I . . I I . . . .. . ... . 0. . Q. .. 0 . . . l. .0...~..‘.I1....9J..l.... ...l. 2 .5 .. . .. 0 .0 00'!
. .0. .. a 0. . .o - 00.. v . . .o .0 .v 0. .0 000 . '0. ..f . I-.)I ...0. 0.2.0.0 ..100. 4.0 .. I0. 0 ...0‘0I *0 ‘00 a )J 0...
,. . . .. .. . . U..- .. 4t. 0.. for
.u. .. .. .... ... . u . .. . . . I . h .. .. o . . . . ... .... .. ... u... .. a J. II“: . ... .... . ..li....u..n.3.0: unr’vmxu.nuo.wno .Vod.a..r..0.50b«u {Apt-£0... .0. In.
I . to . . I I . .. .00 .. . . .I .c . . . . . . . 90' . l; ... 0 a
. 0N. . . 0...... 2 ..0 a . I.. I. .. . ....0. . ... . . .. . 0. 0 ... n: 0 . ., . I .0 I, . .0 . .... .L....q0 . . . . . .. , 00.5.“.‘0.’ no..0hr.ﬁu,”“" 00v} ”Hun-on
. .. . I . 0 . . . I . . a . 0.. .. I .0... . .. . I0 40 0 .‘.A 0. “I. .... . _ . . . . . 0. «I 00.0." ’f'
..0 .. .I ...: . ... ..I .. . . .... .nv no . . -. 0 . 0 . . ... . . - 7. $9130.15! .”u .r 00.10 . . . 0.. . {...-.000 3.0010 .
. . I 0- I .. . v. o I r . . . o. .l 0.. 0- . 0 I o 0 .n. . . u .0 ... ID... I.... ‘ ... . . {’0a0‘03‘n . ..
2. 0| .... . . .. -..I. .. . ... .. .II . . . o. .. I .... ..2. . OI... .u ...I... . . . . . (...00)’ .9903,
. . . . . . J .. .. I . . .2. . . ... .... .. o. . 0. ... o ...} .0. .... .... .. : . . , . . 9. I .Q .013}...
. .0 I . .. c. . L o 00 .. . .. .0.. 0.0.00 . I .. . . . . I .00.)... . .. . O .00 . a. .0. . .0. . 00“. I . . . . . a 600.000....40... '90....
0 - .o a . u c 0 1. 00 . . 0 a ...00. 0 .U o 0 l . I... 0 0. .bu.0 ... .004 . . .. . I. . , y . ..00‘.l..:. ‘ I
0 I o I . v I. . . . I n. I I . I . . . . , ...
o . I . . 0 . V. 0. o . . .304 . .
0. .7. I . 0 I u . .. . . ..0 0... 0'. . .. 0 I . . 00.; 2000» QIIIo0~0‘¢...0 J’ 0,..00‘ﬂﬁi i‘J!.‘o~
. u .. «0. ...... .. .110... .0I...~3.I ..0. ..0 ... . '4 0 . 0 ‘0‘. 9.4.0.: ...Oixi.
. . . . .0..- .. . .....0... 105..--.. ....i... (.... .901. . ,.k0_ .. ..01. l.‘0.lo\.off.\‘
. .... ... . I o . . . I . 04 .H. .3. u. I... ... I... ... . ..II 130....-. I 05 (”10“,... )3. 001'51300'. .
. . .. a .. . .. 2.2.323 .u u ... 5.2.3:...5. .. 5.1.. .48.... ......
o I . v . 0v . I I . . 07' . . u... . .‘2.I.‘.u.. u . w...“ I. ......0’ I Q '00, 0 q. .0 00 .00..” 1‘ 100.0.0 1 0:04000‘
. . c . . . . . . . .... I. . 0.: .0 I . . I . . 1.. 0-0“ .Iv.0\rI.0.av.I.O. la .0. . I .0300. ’.ilv¢f’d~.01
. I. I .. . . I . o . . .41 . 110001..”3 ‘hflwbuﬁ... 65.0.) p.000. 2.500.“: i04..h0:{“u&’~vt.un.l . J5 l.l.0
0 I . - ... . ...- a . ...umo. - . 1... 0 . I. . u... . h .304 u”......u0u.l..9~0.00 2......33010‘40. 40...: .8 ‘20..- I...
.0 . . .0 0. h . ... . _ .. “I..- .. 00 .. .0000]. .0.0 .. coo-......Q‘. .... . o . .50.“.00.0..0.VJ0‘.I. ..0 ’ul 0. 4o
0 . I . o . 0 . .0 .1000: 0. .o 0. .. .I .0 I. v .
. .. u . I .. . I . I .. . I 3000... .I ..I . o .. ... 0......1'4 ..0.,.0u...0..m.ao ......w..¢0nl...0..4100
.. .. .. . . . -I . VI. .. ... .u . .... ............1 .8 .3233:
.. ... . I. . ...... 0.... 0.7!»..0 .100 . . IA;
. I I 0 L 0 .0 o 0 Ev .0 ..\ .0. 0. 00000 .9 .I .0. '“0. CHIC... I!
l. 0 0 .l n. _. I I 0. 0 . . 0 I‘I I .
.0. I. . - .... I . 00 3" 00“.... 0 000 :00.‘.,:.Il...
. .0 n . . . ... . 0 ...“.Ldl-.. 4.0.1.7‘.
. . . 0 . I . o. ..I. .0 0:
. 0I o I I 0 . . . .0 II
.. o . I. .. . . _ .' 0 II . - 0 00
0. .- a
. .. o 0. . . 0
v ..‘0 0 I h ‘ I 00- . .-
I . 0 - I 0 . . .... I 0
I II I . a 0 .. I 0. . II- ..0
. . . I.
. . O ‘0 O
. I . . . . I . ..-
n . . . 0 . .... I. 0 . . v . 00 - 0.: 0... .
- .0 v I ... .0 . a 6. . 0 . I
. .. .. ..0. . .. . . .0: . ..I ... 0. . . 0 n . . . . .
’. .02 .. .‘v0.... .. .03.”.."0 . ' . . O A" .00” t I. . . . 0. 0.”.I . I. I ...“ .0 . . .. .r‘ 0 “.0
...“.h .....Iou...d . .. 0 .... .. ... . _ _ . . 0 . . ...». _ ...... ._ _ . . . I . I. . 0 . ..q
. .. . 0.0!. .....t .. . .. . 0. ... . . .. 0 . . I . .. I .- 0 .04.
'.0 I7... ... 0.‘s¢..0...u.-H.. .. ,7. .. .0 0 ...o. . .. . 0 .0 . . ... . 0 II. . . 0.. 0 . . .. .. . ‘ 0 c0.
. . ..v...v_. .... .I., ... . . _ 0 . 0 _ . . 0 I . c . . . . . ... ... .p . . 0 g 0.. u . A0. 0.0.. . .
. . .. . t . . . . .. . . . . . I. . no . n.
00 0.. I. 0 1 ‘4 0. T ...I 0. ..0. ..I I .. : l... . . . 0.. . ... I . . 0 a QI . . . .l 00 0 I w. 9. J. 0 II . ’01-. 0 |.0. 0 ...0
.. . . oltov. . ., . . ... . . I .. ... q . . . .. 0 . t I .. . . o . 0.. .. 0. . .... . . . . . .. 21...... ...
0 . 0. 0. . ...0 .0.. . . . . . . 0 . . v . 0 0 .. . 0 I . . W. 0 . . . . 0 0 . . . I . .... . ... 00.... .. .. Iou‘.
. . . . .. . . . . . . I . . 0 . I
.0. S... 0 . . . .. 0 . . . . . ... 4.. . .... . .I ”.0 . 0: I0 0 .I0 0 t . on. 0.. IOI.\ I .0...10.0 00 .
0 . C. . 0 .
II. 0 . 0 I 0 . I . I . o. I u. . I . _ I Is 0 .0 0 . ‘JI . a: J . . -.
... . . ,. . . . . . . . . . .. . : - . . . . I. .. . . ... .. II. .....Kpfﬂda In... ...
0 . I . o . . I II . 0 I. . . v. . I 0 .... I . . 0 00 .0. .0: Qt ‘09-'00. ‘.03 I I00. (Ill: .QI’EDth‘ 00.
. . I o I . . I II I . . O . I . . . . 9 I .
nu. . .... . _ .. .. . . . . . I . . ”Q. ~ I r .. . .... 0.01.... . It uV IU‘J..I ".... an. C..0I(0."I.I..3o ‘2"
. . I. - (I: a... ..... . . (...... ..
. .. - . . 0 . . . I . . . I . . 9 . .s . a . .. . 0 I. . 0 o . . 1.. .41.. . I.” ...-.8. ”00... .0.a.t.! .. >.0A.0..alv .30? .0
II.‘ I. . . . u u .. . . r . 0 . 0. 0 .40 v 0 . 0 CA .A 0...‘ I .o D- .OOI‘JIJonN’DI’ 5". ‘ 0 0 0'
00.. 0 0 . 0a..\ 0 .00 0... .I 0. . . .. . . I 0 . . 0 . I __ . o. 0. . 0.0.. 00 K d\ ..01‘ .l O! ... 0000.]. out-0.?d0" '0...
I . 0... . . . I. I. . I u I . . . . . I a. I I0 I . . -0... I
...: .... :1. .....J.... . ......u I. . .. . . . . . . - . .. .. . .. I. . . . u . . . I ......I. ....-. . ......u I r: .-..-.qu
... 0 O 0 .. .. I u o. c 0 l I . 0 . I . g 0 9 u.‘l1.. .. an. ’00. “V. o
I

..l.. . .... ... . ... . ...: . . . .. ... ..IAI : .... . z" ...
gw_§$w.¢...§§.....ﬁﬁ ﬁg.§..a.~§i ......g......._§ ...;

  
 

.. a. . . I r: C. I... . . . Id. XL _‘uw{..w8. ..w . H 1:”. h . o. . .. 0 (PI. ...
gummﬂwﬁlhmén? ... wwaﬂﬂkéwﬂém.23....vwmahuﬁm ...". uh. .....m mumgq$

0 . o
. . ...}... r gag... ..J..§he ﬁg .

I 0 0.. O- .. n. I. . h, . . .
.... . . 1 .. .. s... ... .. 3:31;... .... I ... .0 In..." .III. 2...! .... m...I..~H.... .46.... £10.. be... .. o 1...: . . ... ... . 3.... ..u..r.. . 2...». I 0 ...
. . o u. . I. 0 u. 0

 

 

 

 

' THESIS

1003

This is to certify that the
thesis entitled

CHARACTERIZATION OF METHYLCELLULOSE AND
HYDROXYPROPYL METHYLCELLULOSE IN HIGH-
MOISTURE RESTRUCTURED HAMS

presented by

DEANNA LEA BLOOM-HOFING

has been accepted towards fulﬁllment
of the requirements for the

MS. degree in ANIMAL SCIENCE

 

 

Walnut/M OélpM

Majod Professor’s Signature

5/01 /03

 

Date

MSU is an Afﬁrmative Action/Equal Opportunity Institution

-.-]-I-I-O-l-o-I-0-----l-.-l-

.---t-L...--.--.-.—»-. - - .. - —

Io-u---o---~--v- -.-----I-I-

 

LIBRARY
Michigan State
University

 

 

 

E 'N RETURN BOX to remove this checkout from your record.
TO AVO'D FINES return on or before date due.
' E P ' """ with ear" due date if requested.

CHARACTERIZATION OF METHYLCELLULOSE AND HY DROXY PROPYL
NIETHYLCELLULOSE IN HIGH-MOISTURE RESTRUCTURED HAMS

By

Deanna Lea Bloom-Hoﬁng

A TI-{ESIS

Submitted to
Michigan State University
In partial fulﬁllment of the requirements
For the degree of

MASTER OF SCIENCE

Department of Animal Science

2003

ABSTRACT

CHARACTERIZATION OF NIETHYLCELLULOSE AND HYDROXYPROPYL
NIETHYLCELLULOSE IN HIGH-MOISTURE RESTRUCTURED HAMS

By

Deanna Lea Bloom-Hoﬁng

The objective of this study was to determine if methylcellulose (MC), hydroxypropyl
methylcellulose (HPMC), and kappa carrageenan (KC) would increase cook yields and
decrease purge values. Four hydrocolloid brine treatment (TRT) combinations and a
control (no hydrocolloids) were formulated to produce "test tube" hams. Ham models
were analyzed for purge controlling and textural attributes to determine speciﬁc brines to
be utilized in a commercial study. Five TRTs were formulated for the commercial study:
1) MC 0.4% & KC 0.6%; 2) I-IPMC 0.6% & KC 0.6%; 3) MC 0.4% & HPMC 0.6% &
KC 0.6%; 4) KC 0.6%; and 5) control (no hydrocolloids). Brine solutions (45% addition
wt/wt) were mixed into ground ham (5.33 cm, 2.54 cm and 0.9 cm plate), stuffed into
ﬁbrous casing and thermally processed to 70°C internally. Treatments 1 and 3 increased
(P<0.05) cook yields and were perceived more tender by the sensory panel when
compared to TRT 5. However, TRT 2 decreased (P<0.05) cook yield and purge values.
Treatments 1, 2, 3, and 4 decreased purge values by at least 1.5% when compared to the
TRT 5 while decreasing lightness (L*) values. Trained sensory panel ratings noted TRTs
containing MC and/or I-IPMC to have a slight mouth residue and off-ﬂavor with
decreased juiciness when compared to TRT 4 and 5. Results suggest a hydrocolloid brine
solution containing MC with KC may be a positive purge controller while maintaining

textural and color attributes.

Copyright by
Deanna Lea Bloom—Hofing
2003

This thesis is dedicated to my husband, Josh Hoﬁng. You have been the inspiration, the
motivation and the constant source of support throughout this degree. You never gave up
on me; you picked me up when I was knocked down, and the ﬁrst to congratulate me
when I was successful. I want to thank you for your endless love, support, patience and
last but not least all the hours driving.

iv

Acknowledgments

I would like to thank Dr. Wesley Osbum, my academic advisor, for accepting me
into his program, and believing I could be a masters student when nobody else did. You
have provided me with the tools, skills and conﬁdence to be successful throughout life.
You allowed me to take chances, make mistakes, and learn that there is a reason and
method to research. I can undoubtedly say that I am a better person from this experience.
To my guidance committee: Dr. Al Booren, for all your experience and knowledge, and
allowing me to always ask questions, and helping me through my concerns; Dr. Matt
Doumit, for your positive, happy-go lucky attitude, and your ideas and direction during
my project; and Dr. Gale Strasburg, for your food chemistry advice.

Thanks to my lab mates Christine Quinlan and Jeff Sindelar for their friendship,
help, and patience especially on my bad days. Thanks for all the days of relationship
counseling, sanity discussions and fun. There are no words that can express my gratitude
for them always being there for me helping me through research and life. I will miss you
both; no words can describe how you both have touched my life. To the undergraduate
employees Attalee Hardy and Dan Kiesling for all the 6 am. mornings and your true
dedication to my project. You both treated it as your own project; it would not have been
possible without you. To Linda Steinke, for believing that I could be successful doing
this project. Thank you for all your advice, friendship, and go a get’um attitude. To Tom
F orton and Jennifer Dominquez for your friendships, for taking the time to show me how

to use equipment, for trusting me, and being understanding.

To my Mom and Dad, for always supporting me and pushing me to be the best I
could be. You have instilled in me work ethic, honesty, integrity, and a big heart; virtues
that will make me successful at anything 1 do. Thank you for all the time and love you
gave me over the years, all the years of cattle shows, steer hunting, hay baling, and fence
mending. You will never know how much you both mean to me. Thank you for giving
me the chance to succeed and to make my dreams come true.

And ﬁnally to God, for giving me the strength, courage, perseverance and the
ability to pursue my dreams and for showing me what hardship and failure is along the

way.

vi

TABLE OF CONTENTS

List of Tables .................................................................................................................... xi
List of Figures .................................................................................................................. xii
List of Appendices .......................................................................................................... xiii
Introduction ........................................................................................................................ 1
Chapter 1 ............................................................................................................................ 6
Review of Literature ............................................................................................................ 6
I. Functional Meat Properties ............................................................................................ 6
1. Protein Solubility ............................................................................................... 6
2. Water Holding Capacity .................................................................................... 7
3. Muscle Color ...................................................................................................... 7
4. Firmness, Structure and Texture ........................................................................ 8
5. Connective Tissue .............................................................................................. 8
II. Properties of Water and Water Binding in Raw Meat Products ................................... 9
1. Properties of Water ............................................................................................. 9
2. Water Binding Capacity .................................................................................... 11
3. Added Water ..................................................................................................... 11
III. Properties of Restructured Meat Products .................................................................. 12
1. Color ................................................................................................................. 12
2. Meat Binding and Sliceability .......................................................................... l3
3. Cook Yield and Purge ....................................................................................... 14
4. Textural Attributes ............................................................................................ 15
IV. Functional Properties of Proteins ............................................................................... 16
1. Protein Interactions ........................................................................................... 16
2. Effect of pH ....................................................................................................... 18
3. Addition of Non-meat Ingredients .................................................................... 19
4. Sodium Chloride ............................................................................................... 20
5. Phosphate .......................................................................................................... 21
6. Carrageenan ...................................................................................................... 23
7. Soy Protein Isolate ............................................................................................ 25
8. Modiﬁed Food Starch ....................................................................................... 26
9. Sodium Caseinate .............................................................................................. 27

vii

V. Challenges in Raw Meat Manufacturing of Added Water Meat Products ................ 28

1. Raw Meat Quality ............................................................................................. 28

2. Manufacturing Technologies ............................................................................ 29

3. Color ................................................................................................................. 30

4. Binding Ability ................................................................................................. 30

5. Product Texture ................................................................................................. 31

6. Thermal Processing Yields and Purge .............................................................. 32

VI. Approved Purge Controllers for Meat Products ........................................................ 33
l. Carrageenan ..................................................................................................... 33

2. Soy Protein Isolate ........................................................................................... 34

3. Modiﬁed Food Starch ...................................................................................... 35

4. Sodium Caseinate ............................................................................................. 35

VD. Potential Purge Controllers ....................................................................................... 36
1. Methylcellulose ............................................................................................. 37

2. Hydroxypropyl Methylcellulose ................................................................... 38

VIII. Summary of Literature ............................................................................................. 39
Chapter 2 .......................................................................................................................... 41
Materials and Methods ....................................................................................................... 41

Study 1: Evaluation of methylcellulose and hydroxypropyl methylcellulose in
water and brine solutions.

I. Introduction .......................................................................................................... 41
H. Experimental Design ............................................................................................ 43
III. Hydrocolloid Ingredients ...................................................................................... 43
IV. Manufacturing Process ......................................................................................... 44
a. Solution/Brine Manufacturing ................................................................... 44

b. Meat Model Processing .............................................................................. 45

0. Thermal processing .................................................................................... 45

1. Analyses ................................................................................................................. 46
a. pH Determination ....................................................................................... 46

b. Viscosity Analysis in Hydrocolloid Water and Brine Solutions ............... 47

c. Color Analysis ............................................................................................ 47

(1. Water Retention ......................................................................................... 48

e. Cooked Product Yield and 7-day Purge ..................................................... 49

f. Texture Analysis ........................................................................................ 50

i. Gel Strength/Hardness .................................................................. 50

ii. TPA: 2-Cycle Compression .......................................................... 51

viii

Study II: Evaluation of methylcellulose, hydronrpropyl methylcellulose and kappa
carrageenan in high-moisture restructured hams.

I Preliminary Study H ............................................................................................. 51
H. Study II ................................................................................................................. 53
III. Experimental Design ............................................................................................ 53
IV. Hydrocolloid Ingredients ..................................................................................... 54
V Manufacturing Process ......................................................................................... 54
a. Brine Manufacturing .................................................................................. 54

b. Restructured Ham Processing .................................................................... 55

c. Thermal Processing .................................................................................... 56

(1. Chilling, Slicing, and Packaging Process .................................................. 57

VI. Restructured Ham Storage .................................................................................. 58
VII. Analyses ............................................................................................................. 58
a. Hydrocolloid Brine and Product pH Determination .................................. 58

b. Cook Yield Determination ......................................................................... 58

c. Color Analysis, Lipid Oxidation (TBARS), and Purge Loss ..................... 58

d. Proximate Analysis .................................................................................... 59

e. Texture Analysis ........................................................................................ 59

i. TPA: 2-Cycle Compression .......................................................... 59

ii. Kramer Shear Force ...................................................................... 60

f. Trained Sensory Panel ............................................................................... 61
References .......................................................................................................................... 63
Chapter 3 .......................................................................................................................... 74

Evaluation of hydrocolloid solutions to improve functional attributes of high-moisture
restructured hams in a model system.

I. Abstract ..................................................................................................................... 74
II. Introduction ............................................................................................................... 75
111. Materials and Methods .............................................................................................. 78
IV. Results and Discussion ............................................................................................. 85
V. References ............................................................................................................... 103
Chapter 4 ........................................................................................................................ 105

Evaluation of hydrocolloid ingredients as purge controllers in high-moisture restructured
ham.

1. Abstract ................................................................................................................... 105

ix

II. Introduction ............................................................................................................. 106

111. Materials and Methods ............................................................................................ 108
IV. Results and Discussion ........................................................................................... 117
V. References ............................................................................................................... l 30
Appendices ...................................................................................................................... l 32
Recommendations for Future Research ...................................................................... 163

LIST OF TABLES

TABLE 1: Programmed Water Bath Schedule ................................................ 45
TABLE 2: Smoke House Schedule .............................................................. 55

TABLE 3: Least Square Means for pH, Color, and Gel Hardness of Hydrocolloid Brine
Solutions ............................................................................................. 89

TABLE 4: Least Square Means for pH, Color, and Texture of Restructured Ham
Manufactured with Hydrocolloid Brine Solutions in a Model Meat System,, .............. 94

TABLE 5: Least Square Means for Brine Viscosity, pH, Cook Yield, Color, and 7-day
Purge of a Restructured Ham Manufactured with Varying Combinations of Hydrocolloid

Brine Solutions in a Model Meat System ........................................................ 97
TABLE 6: Least Square Means for TPA of Restructured Ham Manufactured with

Varying Combinations of Hydrocolloid Brines in a Model Meat System ................... 99
TABLE 7: Smoke House Schedule ............................................................ 111

TABLE 8: Least square means for TPA and Kramer shear of restructured ham
manufactured with varying combinations of hydrocolloid brine solutions in a model meat
system ............................................................................................... 117

TABLE 9: Least square means for trained sensory attributes of restructured ham
manufactured with varying combinations of hydrocolloid brine solutions in a model meat
system ............................................................................................... 1 19

TABLE 10: Least square means for TBA analysis, percent purge, and cook yield of
restructured ham manufactured with varying combinations of hydrocolloid brine

solutions in a model meat system ............................................................... 122

TABLE 11: Least square means for color analyses of restructured ham manufactured
with varying combinations of hydrocolloid brine solutions in a model meat system. . .. 124

TABLE 12: Least square means for trained sensory attributes of high-moisture
restructured ham manufactured with varying combinations of hydrocolloid brines. . 1 26

xi

LIST OF FIGURES

FIGURE 1: Study I Flow Diagram ................................................................................... 42

FIGURE 2: Two-way interactions (P<0.01) for pH, viscosity, water retention, and gel
hardness (Exp. 1) ................................................................................................................ 86

FIGURE 3: Two-way interactions (P<0.0001) for viscosity and water retention of
hydrocolloid water solutions (Exp 11) ............................................................................... 88

FIGURE 4: Two-way interactions (P<0.02) for brine pH, brine viscosity, cook yield, and
7-day purge of varying hydrocolloid brine solutions in a meat model system (Exp III)...91

FIGURE 5: Two-way interactions (P<0.0001) for hardness, chewiness, and resilience of

restructured ham manufactured with varying levels of hydrocolloid brine solutions in a
meat model system (Exp HI) .............................................................................................. 93

xii

LIST OF APPENDICES

APPENDIX 1: Water Solution Formulation and Procedures ........................................ 133
APPENDIX 2: Brine Solution Formulation and Procedures ......................................... 134
APPENDIX 3: Combination Hydrocolloid Brine Solution Formulations and

Procedures (Study 1) ........................................................................................................ 137
APPENDIX 4: Programmable Water Bath Procedures ................................................. 141
APPENDIX 5: Viscometer Calibration and Viscosity Determination .......................... 142
APPENDIX 6: TA-HDi Gel Hardness Settings ............................................................ 143
APPENDIX 7: TPA 2-cycle Compression Settings for Meat Model ............................ 144
APPENDIX 8: Proximate Composition ....................................................................... 145
APPENDIX 9: Combination Hydrocolloid Brine Solution Formulations and

Procedures (Study H) ....................................................................................................... 148
APPENDIX 10: Storage Lighting Determination and Conversion Procedure ............... 152
APPENDIX 11: Cook Yield Determination ................................................................... 153
APPENDIX 12: TBAAnalysis ....................................................................................... 154
APPENDIX 13: TPA 2-cycle Compression Settings .................................................... 157
APPENDIX 14: Kramer 5-Blade Shear Settings ........................................................... 158
APPENDIX 15: Trained Sensory Panel Ballot ............................................................... 159
APPENDIX 16: Trained Sensory Panel Sample Randomization ................................... 160
APPENDIX 17: TA-I-IDi Texture Analyzer Calibration and Analysis Procedures ...... 161

xiii

INTRODUCTION

Restructured meat technology provides processors with the opportunity to use
under utilized meats, to manufacture products with speciﬁc sensory and textural
attributes, and portion size with speciﬁc compositional standards (Mandigo 1976; Acton
1983). Examples of restructured products are boneless hams, chicken nuggets, and beef
steak. A key principle of restructured meat technology is the binding of meat pieces
together, resulting in a product with a homogenous “whole muscle” appearance. In order
to bind meat pieces, the meat must be “comminuted” or reduced in size (particle size
reduction). The purpose of particle size reduction is to facilitate the extraction of salt
soluble myoﬁbrillar proteins by increasing surface area (Acton 1983). The addition of
salt and/or phosphate combined with mechanical agitation via tumbling, massaging, or
mixing results in the formation of protein exudate on the surface of the meat pieces. The
protein exudate is a result of cellular disruption of myoﬁbrillar protein and fractm'ing of
the membrane structure which enhances protein extraction, solubilized by salt and
phosphate. The myosin protein exudate is the “adhesive” or “glue” that binds muscle
ﬁbrils, added water, fat, connective tissue and any non—meat ingredients within the meat
matrix (McCormick 1982). The protein exudates form a heat set gel upon thermal
processing resulting in higher cook yields, enhanced bind strength, and improved
tenderness.

Restructuring uses several particle size reduction processes: chunking, ﬂaking, or
chopping (Pearson and Gillett 1996) either singly or in combination. Chunking grinds

cold/ﬁozen meat pieces through larger grinder plates (> 2.54 cm dia). Flaking

comminutes frozen meat pieces into “slices” or “ﬂakes” with the desired particle size.
The ﬂaking process is the result of a high speed rotating impellar that cuts the meat into
thin ﬂakes (Claus and others 1994). Chopping decreases meat particle size at a high rate
of speed utilizing rotating knives in a metal rotating bowl. Most chopping is
accomplished under vacuum to decrease incorporation of air.

Mechanical agitation as previously stated aids in myoﬁbrillar protein extraction.
Tumbling is the rotation of meat and brine in a stainless steel drum with bafﬂes that
agitate meat pieces to extract myoﬁbrillar proteins. Adequate tumbling is important
because it has a direct impact on product quality, texture and appearance (Lin and others
1990). Tumbling can be accomplished with or without vacuum. Vacuum tumbling
extracts air from the system allowing for increased protein-protein interactions that
accelerates protein extraction by “opening up/unfolding” the structure of meat proteins,
allowing easier incorporation of salt and/or phosphate into the meat. Massaging is a
similar process to tumbling but less rigorous. The massaging process involves rotating of
meat pieces against themselves and the surface of the metal drum (Cassidy and others
1978). Mixing is the mechanical incorporation of meat and brine in a metal hopper at
slow speeds by ribbons, paddles, or solid ﬂight agitators. The agitators are horizontally
attached and usually rotate in opposite directions (Hall and others 1986). The mixing
process can also be performed with or without vacuum and mixing speed is adjustable.
Adequate tumbling/massaging/or mixing times are required as improper times can result
in products with poor texture. Mechanically agitating a product too long can result in
rubbery texture from over-extraction myoﬁbrillar proteins and too little can create soft

texture from under-extraction (Lin and others 1990).

Processors must consider raw material quality when selecting ingredients for
restructured meat products. Raw meat materials for restructured products can vary in
species (beef vs. chicken), quality (pale, soft, exudative (PSE) vs. dark, ﬁrm, dry (DFD))
and composition (moisture, fat, and connective tissue). The restructuring process allows
for the inclusion of lower value meat cuts to be formed into a higher value product.
Poorer quality meat products such as PSE pork and DFD beef can contribute to color
variation and instability, cook yield variations and poor meat binding in restructured meat
products (Schmidt and Trout 1984; Trius and others 1994b). Restructuring also allows
for tough pieces of meat with more connective tissue to be utilized due to particle size
reduction (Huffman and Cordray 1982).

Non-meat ingredients are added to restructured meat products to improve water
binding and retention, sensory and textural attributes (Gillett and Carpenter 1992),
particularly in the manufacture of added water restructured products. Water is a unique
di-polar molecule that is attracted to the electrically charged groups of meat proteins
(Aberle and others 2001). This di-polar characteristic provides a basis for water’s
interactions, binding, and water holding capacity (WHC) with the meat proteins. Water
is traditionally a carrier of non-meat ingredients as most are water-soluble or can be
dispensed in water with agitation for subsequent addition to meat (Miller 2000).

Protein- and carbohydrate-based non-meat ingredients, soy protein, sodium
caseinate, starches, carrageenan and methylcellulose can aid in the binding and retention
of larger volumes of added water in restructured meat products. The challenge is to
manufacture a restructured product with adequate water binding, minimal purge (released

water) and acceptable sensory attributes utilizing proper non-meat ingredients to enhance

these properties within the meat system (Osburn 1996). The addition of protein-based
ingredients such as soy proteins results in better binding and improved texture of meat
products (Megard and others 1985; Alvarez and others 1990; Ahn and others 1999). A
carbohydrate-based ingredient such as modiﬁed food starch reduces cooking losses,
improves sensory attributes, and textural cohesiveness (Troutt and others 1992). The use
of hydrocolloid gums, such as carrageenan improves water holding capacity, uniformity,
Sliceability, and texture (Trudso 1985). Additionally, methylcellulose (MC) and
hydroxypropyl methylcellulose (HPMC) are hydrocolloid gums that have some purge
controlling attributes (Steinke 2001) in addition to improved tenderness and juiciness
attributes (Hill and Prusa 1988; Mittal and Barbut 1993; Steinke 2001).

This thesis research was conducted in two studies. The objective of Study I was
to investigate the effects of MC, HPMC, and kappa carrageenan (KC) individually on
water binding, water retention and quality characteristics in water solutions, brine
solutions, and a restructured high-moisture ham model meat system. This study
determined the hydrocolloid type(s) and levels that may enhance product properties when
used in high added water restructured meat products. The objective of Study II was to
investigate the effects of incorporating hydrocolloid brine solutions into a high-moisture
(45% added water) restructured ham product on cook yield, purge, sensory and textural
attributes.

This thesis is formatted as four chapters. Chapter 1 is the review of literature.
Chapter 2 covers in detail, the materials and methods used in Study I and II. Appendices

are provided with step by step procedures for all protocols and procedures used for each

study. Chapters 3 and 4 are presented in a scientiﬁc manuscript format according to the

Journal of Food Science style guide.

CHAPTER 1

LITERATURE REVIEW

1. Fresh Meat Properties

Functional properties are deﬁned as the physical or chemical properties within
meat proteins that affect their behavior during processing, storage, and consumption
(Kinsella 1976; Smith and Culbertson 2000). Functional properties affect product quality
and sensory attributes, thus the understanding of proteins’ principal components (myosin,
actin, other myoﬁbrillar proteins) is necessary. They also dictate the protein’s usefulness
to the processor, its appeal to the consumer and its ability to be further processed (Aberle
and others 2001). Fresh meat protein properties of particular importance are protein
solubility, water-holding capacity (WHC), color, and structure, ﬁrmness and texture.

Solubility of meat proteins is determined primarily by the amino acids on the
surface as well as external factors such as pH and salt addition (Smith and Culbertson
2000). The pH of the meat at the isoelectric point (IP) of 5.0 is ideal for myosin protein-
protein interactions. At the IP negative and positive charges of proteins (myosin) are
equal, which increases protein-protein interactions and decreases protein-water
interactions. A decrease in WHC and textural quality is seen in meat at the IP. At a pH
range above or below the IP (5.0) electrostatic repulsion between protein molecules
increases and solubility is enhanced. Protein solubility is also a ftmction of salt
concentration. As salt concentration is increased. solubility of meat protein will increase,

thus allowing for increased WHC due to the extraction of myosin. Salt at a concentration

of about 6.0% solubilizes myosin proteins (Frank 2000) although, typically, 1.5 to 3.0%
salt is added to cured meat formulations. The addition of salt allows for meat proteins to
swell up to twice their normal size by binding the chloride ion to the protein ﬁlaments.
Binding with the chloride ion shifts the isoelectric point and increases electrostatic
repulsive forces between proteins (Offer and Trinick 1983; Lewis and others 1986;
Belton and others; 1987; Miller 2000). The repulsive forces allow proteins to unfold and
then swell. The swelling of the proteins provides a higher ntunber of side chains
(Lindsay 1985) that can bind water and increase WHC.

Water-holding capacity (WHC) is the ability of meat to retain endogenous or
added water during application of external forces such as grinding, heating, cutting or
pressing (Hedrick and others 1989; Aberle and others 2001). Raw meat color, texture,
ﬁrmness, cooked meat juiciness, and tenderness are all dependant on WHC. During
normal slaughter and fabrication processes where carcasses are subjected to chilling,
generated adenosine triphosphate (ATP) and glycogen converted to lactic acid causes
muscle pH to fall from 7.4 to an ultimate pH of 5.4 -5.8 (Hedrick and others 1989; Aberle
and others 2001). This drop in pH and onset of rigor alters cellular and extracellular
components which contribute to WHC (Offer and Knight 1988). Water holding capacity
is also dependant upon bound, immobilized, and free water within the muscle tissue
(Northcutt and others 1994). For this reason, processors focus on retaining these
different forms (bound, immobilized, free) but primarily free water with non-meat
ingredients such as salt and phosphate.

Muscle color is an impression seen by the eye and is dependant upon the light

source as well as the consumer (Aberle and others 2001). Consumers relate the color of

raw meat with freshness (Adams and Huffman 1972). Color also varies with the type of
processing method utilized such as cured versus uncured and raw versus cooked.
Myoglobin is the primary pigment found in muscle. Myoglobin consists of a globular
protein portion called globin and a non-protein moiety called heme. The degree of
myoglobin present in muscle varies within species of animal, age, sex, and muscle type.
For example, as the chronological age of the animal increases, the quantity of myoglobin
in muscle increases resulting in a darker meat color (Kauffrnan and Marsh 1987). This
darker color (age or DF D) creates less consumer appeal in a raw meat product (Nold and
others 1999).

Rigor state, intramuscular fat and connective tissue content contribute to meat
ﬁrmness, structure and texture. As muscle is converted to meat there is progressive
rigidity to the muscle ﬁbers. This creates increased ﬁrmness because of rigor mortis, and
solidiﬁcation of fat within muscle (Aberle and others 2001). Yet, with carcass aging
there is increased enzymatic degradation improving tenderness and palatability. Muscle
structure is related to WHC. Muscle tissues with poor WHC exhibit a soft, loose
structure with a grainy texture compared to tissues with greater WHC which exhibit ﬁrm
structure and dry texture (Lin and others 1990; Aberle and others 2001). Furthermore,
intramuscular fat “marbling” has a positive effect upon muscle ﬁrmness and texture,
ﬂavor and juiciness. Wood (1985) suggested that leaner pigs have an increased
likelihood of drier, less juicy products.

Collagen connective tissue contributes to meat toughness and overall texture of
meat products (Whiting 1989). Older animals and muscle groups used for locomotion

(chuck, round) have high numbers of insoluble collagen cross-links (Bailey 1984). The

restructuring process including particle size reduction allows for a decrease in detectable
amounts of collagen when restructured steaks were evaluated by a sensory panel (Booren
and others 1981). For example, 12-30% of consumers determined that restructured steaks
manufactured with a high amount of gristle (16.4 mg/g total collagen) were acceptable
but not preferred over low-gristle steaks (9.4 mg/ g total collagen) (Berry and others
1988). Furthermore, trained panelists found blade tenderized. restructured roasts with
high amounts of collagen (17.91 mg/g) to be less ﬂavorﬁrl, juicy, and tender than

trimmed steaks with less (11.13 mg/g) gristle (Flores and others 1986).

II. Properties of Water and Water Binding in Raw Meat Products

The ability of meat to hold water during processing, packaging, storage and
ultimately consumption is critical. Important functional properties that determine
ﬁnished product quality include water binding and water holding ability of the meat
product (Whiting 1988). Water holding capacity (WHC) is necessary not only ﬁ'om an
economic standpoint for the meat processor (higher yields) but also for the consumer
(more palatable, juicier product). The amount of water added and its classiﬁcation
(bound, immobilized, or free) within meat profoundly inﬂuences meat quality (Northcutt

and others 1994).

Properties of Water
Water is a unique di-polar molecule that is attracted to the electrically charged
groups of meat proteins (Aberle and others 2001). This di-polar characteristic provides a

basis for water’s interactions and binding with the meat proteins. Water comprises 75%

of skeletal muscle, four times greater than any other chemical component of meat. The
functional properties of muscle proteins rely largely on their ability to bind and retain
water (N orthcutt and others 1994).

Water in meat is classiﬁed as bound, immobilized, and free, according to its form
of muscle ﬁber binding (Hamm 1972; Honikel 1987). Bound water is 4-5% of total
water in muscle tissue (Aberle 2001; Anonymous 2003. It is associated with the surface
of proteins by dipole-dipole interactions and hydrogen bonds to form a single layer on the
surface of the protein binding to the muscle ﬁbers. Bound water is never released from
muscle tissue even if processed (heated, frozen, freeze dried, etc.) because it is held
tightly to the muscle ﬁbers.

Immobilized water is 16-17% of the total water in muscle tissue. Juiciness of
meat products is deﬁned by the amount and state (room temperature vs. heated vs.
frozen) of immobilized water (Borisova and Oreshkin 1992). Immobilized water is not
bound as tightly to the protein molecules; it is released during processing and is aﬁ‘ected
by environmental conditions such as heating, cooling, and pH. Immobilized water
inﬂuences the product’s ability to retain water during processing.

Free water comprises the largest percentage of total water in muscle at 79%.
Capillary forces hold the free water with limited ordering of their molecular structure and
their orientation is highly independent of the charged groups (Anonymous 2003). Free
water is easily lost via “weep” or “drip” in fresh cuts of meat, or purge in vacuum packed
processed products (Hedrick and others 1989). For this reason, processors focus on
binding free water by increasing protein hydration with different forms of non-meat

ingredients such as salt and phosphate.

10

Water Binding Capacity

The terms water binding capacity (WBC) and water-holding capacity (WHC) are
commonly used interchangeably throughout literature. They are deﬁned as the amount of
water that is bound or retained by myoﬁbrillar proteins with the application of external
forces such as cutting, heating, grinding, or pressing (Hedrick and others 1989; Smith and
Culbertson 2000; Aberle and others 2001). Water binding capacity determines raw meat
and cooked meat quality through the binding of tissue water and added water with
myoﬁbrillar proteins (Hamm 1960, 1985, 1994; Offer and Knight 1988). Altering of
cellular and extracellular components due to changes in pH, onset of rigor, and carcass
aging each affect WBC (Offer and Knight 1988) and can change the meat’s functional
properties (Northcutt and others 1994). Furthermore, the development of heat-set protein
gel during thermal processing, from extracted myoﬁbrillar proteins, can also contribute to
water binding and retention abilities of the ﬁnal product (Asghar and others 1985).
Water holding capacity in turn has an inﬂuence upon cook yields, purge, color, and even

texture of the ﬁnal product.

Added Water

Water is the cheapest non-meat ingredient source ideal for increasing the
proﬁtability of meat products for processors. Of all the non-meat ingredients, water
constitutes the largest percentage and, as a result, it is almost always listed ﬁrst on the
ingredient label in water added meat products. Speciﬁc product labeling must deﬁne the

amount of water added in order for the meet USDA-F SIS approval (Miller 2000).

11

Added water in conjunction with non-meat ingredients assists in reducing cook
loss and compensates for moisture typically lost during thermal processing of a meat
product (Romans and others 1994). It is traditionally a carrier for non-meat ingredients
as most non-meat ingredients are water-soluble or can be dispensed in water with
agitation for subsequent addition to meat (Miller 2000). However, the addition of water
may have a negative impact on meat ﬂavor and shelf-life. Water dilutes out the meat
ﬂavor and increases water activity, therefore, provides more free water for microbial
growth. The increase of microbial growth decreases meat shelf-life. Furthermore.
Prabhu and Sebranek (1997) stated that as the amount of added water increases in
restructured meat products, the ability to retain water during thermal processing and
minimize purge during storage decreases without the use of purge controllers. Claus and
others (1990) demonstrated that the addition of high amounts of water (30%) decreased

bologna product ﬁrmness, cohesiveness while increasing cook loss and purge.

III. Properties of Restructured Meat Products.

Color

Color is the hue (red, green, blue, etc.) that is detected by the eye. The color of
meat products is a prime factor by which consumers judge their acceptability and product
selection (Secrist 1982; Chen and Trout 1991). Myoglobin is the primary muscle
pigment and the degree of myoglobin present in muscle varies with species of animal,
age, sex, and muscle type. Furthermore, the use of lower quality meat raw materials such

as PSE pork, can decrease cook yields, meat binding, and decreased color perception

12

(Wismer-Pederson 1960a, 1960b; Davis and others 1975; Jerimiah 1986; Honkavaara
1988 1990). Shand and others (1995) proved that utilizing PSE pork in cured bone-in
ham signiﬁcantly decreased cook yields, juiciness, ﬂavor, and developed a lighter cured
color. It has been shown that the addition of water dilutes the myoglobin (Miller 2000)
which results in a paler product color. Akamittath and others (1990) have also
demonstrated that restructured beef streaks manufactured with 1.5% salt displayed higher
color instability and fat oxidation when compared to treatments with phosphate (0.2%)
and tocopherol (0.02%). In another study, restructured beef steaks manufactured with
salt (1.0%) and phosphate (0.5%) initially demonstrated the highest color scores (more
red color) initially but after a 12 week storage time had the lowest color scores (more

brown) when evaluated by a trained panel (Chen and Trout 1991).

Meat Binding and Sliceability

Restructured meat processing procedures such as chunking, grinding, mixing or
tumbling allow for efficient brine migration into the meat, enhance the extraction of salt
soluble myoﬁbrillar proteins and increase meat protein binding (Krause and others 1978;
Ockerman and Organisciak 1978). Yet, to achieve adequate meat protein binding in
restructured added water ( 1 0-40%) meat products the proper selection and addition of
non-meat ingredients is critical. Non-meat ingredients are used to improve protein
binding and WHC in processed meat products (Maurer 1979). In addition, they are also
used to increase protein content, fat binding properties, or slicing characteristics (Pearson
and others 1996). For example, restructured hams containing soy protein isolate (SP1)

were formd to have higher meat binding strength than control hams (Siegel and others

13

1979). Alvarez and others (1990) found that the addition of starch (30%) signiﬁcantly
increased meat binding. shear values, and tensile strength when compared to SP1 (10%)
in restructured mechanically deboned chicken. These beneﬁcial properties of non-meat
ingredients allow for increased product quality and consumer satisfaction. Furthermore,
Shand and others (1994) demonstrated that while cooking temperature had no signiﬁcant
effect (P<0.05) on meat binding in restructured beef rolls, the addition of higher levels of
kappa carrageenan (0.5-1.0%) improved binding shown by increased hardness and force
to fracture results. Oven roasted turkey breasts containing 0.5% kappa carrageenan (KC)

had higher Sliceability values than the control turkey breasts (Bater and others 1992).

Cook Yield and Purge

Addition of water to restructured meat products results in “extending” meat
proteins and increasing product cook yields (Prabhu and Sebranek 1997). Due to the
increased use of purge controllers such as SP1 and KC, cook yield values are rising
considerably. Although water may be bound during the cook process, SP1 and KC may
not have the ability to retain the water once packaged. Purge is the loss of water released
during storage, which is mostly seen in the product’s package at the retail case. This
results in consumers shying away from products that have poor appearance due to high
amounts of released ﬂuid in the package (Chen and Trout 1991). Siegel and others
(1979) demonstrated that water binding induced by SPI increased cook yields and
enhanced the meat-to-meat binding by minimizing the effect of excess water on extracted
myoﬁbrillar proteins (Siegel and others 1979). Shand and others (1994) reported

signiﬁcant decreases in purge values when utilizing KC at 0.5% and 1.0% in structured

14

beef rolls. Furthermore, Prabhu and Sebranek (1997) also demonstrated a signiﬁcant
decrease in purge values utilizing KC at 1.5% in ham. However, there is still
considerable use of conventional brine solutions (salt, phosphate, cure) that result in
lower cook yield values and higher purge values. Acton (1983) found that a traditional

brine solution dilutes protein exudates which resulted in decreased cook yields.

Textural Attributes

Texture is a dominant quality characteristic in cooked meat products (Boume
1982). Textural attributes such as hardness, cohesiveness, and chewiness can be
evaluated by a sensory panel (trained, semi-trained, or consumer) or mechanical device
(texture analyzer). The addition of water creates a meat protein dilution effect resulting
in a softer textured product (Claus and others 1989). Yet, the addition of non-meat
ingredients has allowed for an increase in textural attributes. The addition of
carrageenan, SPI, phosphates, and salt improves product texture. DeFreitas and others
(1997) noted that the addition of KC at 0.5% increased hardness of cooked linked pork
sausage when compared to those with no KC. Improved textural attributes such as
hardness, binding, and force to fracture values were also documented for structured beef
rolls with 0.5%-1.0% KC (Shand and others 1994). Furthermore, beaker pork sausage
manufactured with 0.5% KC had increased ﬁrmness values (Trius and other 1994b).
Textural improvements in restructured meat products is necessary as they are conveying
the importance of meat and water binding to make a cohesive, texturally acceptable

product.

15

IV. Functional Properties of Proteins.

Protein Interactions

The production of restructured meat is dependent upon water, fat, and protein
binding during processing for acceptable texture after thermal processing. The myosin or
actomyosin proteins must be suspended, solubilized, denatured and then aggregated by
heat (Gaska and Regenstein 1982; Acton and Dick 1984; Ziegler and Acton 1984) to
form a cohesively bound ﬁnished meat product. The functionality (hydration/solubility)
of myosin during meat processing has a direct impact on yield, texture, moisture and
appearance. In the manufacturing of “emulsion type” products the formation of a stable
meat batter is the balance between protein-water and protein-protein interactions
(Whiting 1987). Meat binding properties can be divided into three categories: 1) protein-
water interactions, 2) protein-fat interactions, and 3) protein-protein interactions. These
interactions are also inﬂuenced by types and amounts of non-meat ingredients added to
the formulation and by the processing conditions used (Shand and others 1993; Smith
2001). For example, non-meat ingredients such as salt, soy protein and carrageenan
increase meat binding, WHC, and texture by extracting myoﬁbrillar proteins ﬁ'om the
meat to serve as a binder between the meat pieces (Siegel and Schmidt 1979). These
non-meat ingredients enhance protein-water and protein-fat interactions thus increasing
product yields by creating a network between the meat protein and the non-meat
ingredient.

The ability to bind and retain added water is an important functional attribute in

meat products. To increase the meat product’s WHC, protein-water interactions need to

16

be optimized. In order to enhance and maintain protein-water interactions, protein
extraction and solubility are necessary. The most important meat proteins for WHC are
the salt-soluble proteins (Gillett and others 1977) that are extracted with typical salt
levels of 1.5-3.0% in processed meat products; although higher levels (4-8%) may be
used for dry-cured hams and sausages. As the concentration of salt is increased (1.0 vs.
1.5%) the sodium and chloride ions bind to the charged groups on the protein ﬁbers and
weaken the intermolecular interactions between muscle ﬁbers (Smith and Culbertson
2000). This exposes more water binding sites which increases protein-water interactions
and decreases protein-protein interactions. If meat proteins are not solubilized during
extraction the ﬁnal cooked product has poor water binding and a brittle texture (poor
Sliceability). Additionally, the pH and temperature during processing affects the
extractability of muscle proteins. To optimize myoﬁbrillar protein extraction, a pH of
approximately 6.0 (Solomon and Schmidt 1980; Dutson 1983) and a temperature between
2-4°C are needed (Osburn 2001).

Protein-fat interactions are important because fat impacts product ﬂavor, texture
and mouth-feel. Protein and fat droplets bind together and create a cross-linking matrix
between protein and fat that helps lock in moisture by forming a hydrophobic bridge that
seals in water. This matrix gives the meat product a smoother, ﬁrmer texture, and added
juiciness. However, the degree to which protein-fat interactions are needed for ﬁnished
product quality is still being investigated. Areas and Lawrie (1984) reported that further
research is required to determine the degree of protein-lipid interactions to maximize

protein-water and protein-protein interactions.

17

Protein-protein interactions can create adverse ﬁnished product attributes.
Myoﬁbrillar proteins “prefer” protein-protein interactions resulting in poor product
texture, increased purge and tough texture (Uram and others 1984; Hand and others 1987;
Claus and others 1989). The pH of the meat at the IP of 5.0 is ideal for myosin protein-
protein interactions. At the IP negative and positive charges of myoﬁbrillar proteins are
equal, which increases protein-protein interactions and decreases protein-water
interactions. Therefore, a decrease in WHC and textural quality is seen in the meat
product. However, there are processed meat products that require lower pH values
resulting in increased protein-protein interactions. Dry sausages such as pepperoni and
summer sausage require a pH lower than 5.0 to increase product ﬂavor and decrease
water content. As the pH moves away from the IP, there is a decrease in the number of
protein-protein interactions and an increase in protein-water interactions allowing for
improved product quality.

For the formulation of a quality processed meat product all three properties
(protein-water, protein-fat, protein-protein) must be taken into consideration when
selecting ﬁnal product qualities. Each of the properties are equally important in meat

processing, with protein-water interactions being the most inﬂuential on increased WHC.

Effect of pH

The pH of meat is important as it inﬂuences the WHC, texture and tenderness of
meat (Dutson 1983). The pH at which the WHC is at its minimum (~5.0) corresponds to
the IP of myosin as well as the myoﬁbril (Offer and Knight 1988). The net charge of the

myosin is at its minimum (0) which increases bonding between the proteins. This

18

increase of protein-protein interactions decreases protein solubility and its ability to bind
with water and create protein-water interactions. To increase muscle water binding, the
pH of the proteins must move away from the [P which increases electrostatic repulsion
between protein molecules thereby enhancing protein solubility. At higher pH levels, the
proteins become more negatively charged, thus repelling each other and allowing for the
myoﬁbrillar proteins to swell and retain water, resulting in increased WHC (Hamm 1994;
Osburn 2001). To create a more optimum environment for both water binding and
protein solubility, non-meat ingredients can be added to the meat product. For example,
sodium tripolyphosphate (STP) can adjust the meat pH protein net charge (-OH) toward
the alkaline side of the pH scale and improve the meat’s water binding ability due to an
increase in pH. In general, a pH at 6.0 is the most effective at increasing water and
processed meat binding. At pH 6.0, the gelling and binding of proteins myosin and

actomyosin is ideal (Dutson 1983).

Addition of Non-meat Ingredients

To manufacture restructured meat products with acceptable textural attributes
meat processors utilize non-meat ingredients/additives such as salt, phosphate, KC, SP1,
and starches. Non-meat ingredients are deﬁned as any type of non-animal based
ingredient that is allowed as an additive in meat products by the United States
Department of Agriculture (USDA), and the Food Safety and Inspection Service (FSIS)
(Pearson and Gillett 1996). They are added to fresh or processed meat product
formulations to improve juiciness and/or tenderness, enhance ﬂavor, stabilize or improve

color, increase shelf life, control microbial growth, or increase the WHC of a product

19

(Miller 2000). In addition, they are also used to increase protein content, improve
emulsion stability, fat binding properties, or slicing characteristics (Pearson and Gillett
1996). These beneﬁcial properties of non-meat ingredients allow for increased product

quality and consumer satisfaction.

Sodium Chloride

Sodium chloride (N aCl) or salt was historically added to meat for preservation
purposes when refrigeration was not available. For this application, high levels of salt
were either rubbed on the exterior surface or attained by placing the meat into a highly
concentrated salt brine for an extended period of time (Miller 2000). The high level of
salt decreases water activity, consequently reducing microbial growth and rancidity that
contributes to spoilage (Romans and others 1994). However, sodium reduction has been
recommended in human diets to decrease hypertension, stroke and renal failure (Sebranek
and others 1983). Although the decrease of salt is associated with decreased health risks,
it has adverse effects on processed meat quality. Reducing salt by 40% in a frankfurter
batter caused an extensive loss of water binding ability and reduced gel strength (Whiting
1984)

Salt is an important ingredient in processed meat products for three primary
reasons: 1) it solubilizes proteins to create desired texture, 2) it provides ﬂavor, and 3) it
controls microbial growth (Ingram and Kitchell 1967; Rust and Olson 1988). Salt, at a
concentration of about 6.0%, solubilizes myosin proteins (Frank 2000). Typically, 1.5 to
3.0% salt is added to cured meat product formulations, with the bulk of the salt added

initially to the meat block. This allows the salt soluble myoﬁbrils to swell to twice their

20

normal size by binding the chloride ion to the protein ﬁlaments. Binding with the
chloride ion shifts the isoelectric point (-OH) and increases electrostatic repulsive forces
between proteins. The repulsive forces allow proteins to unfold and then swell. The
swelling of the proteins provides a higher number of side chains (Lindsay 1985) that can
bind water and increase WHC. Hamm (1981) showed that salting prerigor or postrigor
sausage formulations increased WHC. Furthermore, improved WHC, cooked color
scores, and sensory attributes were seen in restructured pork products with 0.75% salt

(Schwartz and Mandigo 1976).

Phosphate
Phosphates manufactured from salts of phosphoric acid, include orthophosphates
with a single phosphorus atom and polyphosphates with two or more phosphorus atoms
(Shirnp 1981; Sofos 1986). The basic chemical function of phosphate is to control pH by
acting as a buffer to sequester metal ions and increase ionic strength of solutions
(Halliday 1978; Steinhauer 1983). Phosphates sequester the ions and increase ionic
strength by acting as a polyvalent ion. As the ionic strength of the phosphate increases,
the phosphate anions align with oppositely charged groups of proteins, and cause more
repulsion between protein molecules which increases the volume of open ﬁlament spaces
(Barbut and others 1988). This repulsion subsequently enhances WHC by allowing the
increase water volume within the protein structure. The allowable limit for phosphates in
meat products is 0.5% of the ﬁnished product weight (U SDA-F SIS 2002).
Of the phosphates used in the meat industry, STP is the most popular. They

account for 80% of the phosphates incorporated either as a single phosphate or in blends

21

(Barbut and others 1988). Phosphates inﬂuence water binding, color, texture,
coagulation, emulsiﬁcation, and microbial growth as a result of their chemical effects and
reactions with food components (Barbut and others 1988; Dziezak 1990). The addition
of about 0.4% polyphosphates to comminuted, cured meat products such as sausages,
frankfurters, and bologna, accelerates cure color development, improves protein binding,
stabilizes emulsions to prevent fat cook-out, and reduces requirements for curing
ingredients (Dziezak 1990). Adding phosphates to cured meat and frozen whole meat
decreases the loss of natural juices that occurs from the slaughter to packaging (Dziezak
1990). Fresh meat’s loss of natural juices from slaughter to packaging leads to tough
texture, reduced juiciness, and susceptibility to freezer burn. When used with salt,
phosphates can increase water binding or retention of the fresh meat’s immobilized and
free water. Additionally, restructured pork products with STP levels of 0.125 to 0.5%
improved WHC, while decreasing cook loss and package purge (Schwartz and Mandigo
1976)

Phosphates also enhance sensory characteristics of meat products such as
tenderness, overall acceptability, and reduction of warmed-over ﬂavor (Smith and others
1984; Jones and others 1987). Pork roast containing added phosphates were judged by
sensory panelists to be more tender, and juicy, with less off-ﬂavor and more palatability
than roasts containing acetic acid, sodium ascorbate or the control (Boles and Parrish
1990). Sensory panelists evaluating restructured pork found that STP at 0.375%
signiﬁcantly (P<0.01) improved eating texture and ﬂavor when compared to restructured
pork with 0.5% STP (Schwartz and Mandigo 1976). Phosphates also help prevent the

development of off-ﬂavors and off-odors by inhibiting rancidity in processed meats

22

(Ellinger 1972). For example, when added to ground pork patties it reduced
thiobarbituric acid (TBA) values, a common measurement of lipid oxidation (Keeton
1983; Miller 2000). Further research also showed that lipid oxidation could be inhibited
in restructured beef, pork, and turkey steaks for 4, 6, and eight weeks respectively with
the use of phosphates at 0.3%. However. off-ﬂavors have been reported when
phosphates were added to meat products. When STP was added to beef and pork roasts,
panelists sometimes detected a metallic and soapy ﬂavor (Smith and others 1984; Vote
and others 2000). Samples with 0.5% phosphate were signiﬁcantly more soapy than

samples without or with lower levels of phosphate (Craig and others 1991).

Carrageenan

Carrageenans are hydrocolloids composed of sulfated linear polysaccharide units
extracted from red seaweeds. The polysaccharide chain of carrageenan consists mainly
of potassium, sodium, magnesium, calcium, and ammonium sulfate esters of galactose
and 3,6—anhydrogalactose copolymers (Glicksman 1969; Glicksman 1983). They are
generally recognized as safe (GRAS) by the United States Food and Drug Administration
(FDA). During enhanced meat processing, the processes in which a percentage brine
solution is added to increase meat functionality, carrageenan is ﬁrst dispersed within a
brine solution, introduced into the meat by injecting or mixing, and ﬁnally dissolved
within the meat by thermal processing. The carrageenan solution together with meat
forms a ﬁrm and cohesive gel structure with the meat protein upon cooling (Trudso
1985). This gelling capability makes carrageenan particularly suitable for processed meat

products by improving WHC, consistency, Sliceability, and texture of meat and poultry

23

products especially with high levels of added brine (Trudso 1985). Carrageenan forms a
stable structure above pH 7; it degrades slightly at pH 5-7 and degrades rapidly below pH
5.

Three major available types of carrageenan are designated kappa, iota, and
lambda. Kappa and iota form thennoreversible gels upon heating and cooling and
lambda is a nongelling gum, typically used as a thickener. Additionally, at least four
other types of carrageenan are recognized: mu, nu, theta, and xi (Trius and Sebranek
1996) but these types are not used in the commercial meat industry at this time.

Kappa carrageenan (KC) has alternating 1, 3 linked D-galactose 4-sulfated and
1,4 linked anhydro-D-galactose units. Kappa exhibits gelling capacity with a greater
sensitivity to potassium to form stronger gels. However, these gels are brittle and apt to
undergo syneresis. Brittleness can be reduced by the addition small amounts of locust
bean gum (Daniel and Weaver 2000) and other non-meat ingredients such as NaCl,
potassitun chloride, STP. In order to solubilize KC, heat is applied which then creates a
gel upon cooling. The KC begins to solubilize and swell at 46°C, completely solubilizes
at 66°C, and then starts to gel with the meat proteins when cooled to 44°C (Trius and
Sebranek 1996).

Iota carrageenan (IC) is composed of alternating 1,3-linked D-galactose 4-sulfate
and 1,4 linked 3,6 anhydro-D-galactose 2-sulfate. It forms more elastic gels than kappa
in the presence of potassium cations (T rius and Sebranek 1996). Yet, when calcium
cations are present, IC forms relatively strong gels in contrast to KC, which forms weak

gels (Rees 1972). Neither iota nor kappa carrageenans are found in pure form, but rather

24

as mixtures. As a consequence. a small amount of IC is present with KC and vice versa
(Trius and Sebranek 1996).

Lambda carrageenan (LC) has 1,3 linked D-galactose 2-sulfate and 1,4 linked D-
galactose 2,6 disulfate units. Aqueous solutions of LC are viscous but do not gel (Rees
1969) due to the lack of the 3,6-anhydro-D-galactose units as found in kappa and iota
carrageenan (Rinaudo 1988). Additionally, LC is the only type of carrageenan that is not

hot water soluble.

Soy Protein Isolate

Soy protein isolate (SP1) is one of the most useful non-meat ingredients (Siegel
and others 1979). The major utilization of SP1 is to extend meat products with less
expensive materials (i.e. water) without introducing egregious ﬂavors, or decreasing the
binding quality of the ﬁnal product (Siegel and others 1979). Soy protein isolate is made
ﬁ'om dehulled and defatted soybean ﬂakes (Soy Protein Council 1987). The defatted
soybean ﬂakes are then treated with mild alkali to the extract protein. It is then
centrifuged to remove the insoluble ﬁbrous residue from the protein. The protein
precipitate is conditioned by washing it multiple times and then spray dried to yield SPI
(Soy Protein Council 1987). This process results in an isolate that is at least 90% protein
with increased digestibility (91-96%) and with increased palatability (Mustakas and
Sohns 1976; Soy Protein Council 1987). For example, increased palatability was seen in
a study utilizing SPI, taste panelists preferred turkey rolls extended with SP1 over non-

extended turkey rolls (Kardouche and others 1978).

25

Soy protein isolate is compatible with a wide range of processing equipment and
procedures. It is easily dispersed and increases brine retention in meat products. The
United States Department of Agriculture (USDA) permits up to 2% added SPI
individually or collectively with other approved extenders such as soy protein concentrate
or non-fat dry milk (Soy Protein Council 1987). When SP1 is used, 2% addition of SP1 is
equivalent to 3.5% of other soybean products such as concentrate, ﬂour and grits.
Hawley and Tuley (1976) developed a method of introducing SPI into the brines
commonly used in the production of cured meat items (Siegel and others 1979). After
brine injection, massaging/tumbling is required to distribute the brine uniformly
throughout the muscle. Solubilized SPI used in this manner increases cook yield by 30%
or more while maintaining a protein content of at least 17% as proposed by the USDA for

combination meat products (Siegel and others 1979).

Modiﬁed Food Starch

Starch has traditionally been used in meat products to improve quality and to
extend the more expensive meat fraction of the product (Skrede 1989). It is a low cost
approved ham purge controller that has minimal ﬂavor, especially when compared to SP1.
Starches are polysaccharides that consist of repeating glucose units. Starch molecules
have one of two molecular structures: a linear structure, known as amylose; and a
branched structure known as amylopectin (Hegenbart 1996). Amylose and amylopectin
associate through hydrogen bonding and arrange themselves radially in layers to form
granules of starch. Granule size and shape can change greatly due to type of starch and

degree of chemical modiﬁcation. For example, the size of a starch granule can range

26

from 3 microns to over 100 microns. Furthermore, countless varieties of starches can be
isolated from many different sources such as corn, potato, rice, tapioca and wheat. The
chemical modiﬁcation process for potato starch cross-binds phosphorous groups, and
masks hydroxyl groups with acetyl groups (Skrede 1989). This results in changed
molecular properties and functionality (Howling 1980). In addition, each type of starch ‘
differs in amylose and amylopectin content as well as granule size and structure.
Generally speaking, the amylose gives gel strength and the amylopectin gives high
viscosity to solutions. Amylose structures can easily align themselves and associate
through hydrogen bonding to form gels (Hegenbart 1996). On the other hand,
amylopectin molecules cannot align as easily, thus giving weaker gel strength and less

hydrogen bonding.

Sodium Caseinate

Sodium caseinate (SC) is a milk protein. Casein and its caseinate derivatives have
functional and nutritive properties which make them useful worldwide (Southward 1985).
In addition to availability and high nutritive value, they provide smooth texture and bland
ﬂavors (Konstance and Strange 1991; Keeton 2001). Dairy/milk proteins are not to
exceed 3.5% by weight of ﬁnished products to be labeled as meat. (Frank 2000). Sodium
caseinate contains 90% protein, is completely water soluble, absorbs at the fat/water
interface in meat emulsions, contributes signiﬁcantly to binding and ﬁrmness, but has no
gelation capabilities (Anonymous 2001). In addition, SC’s are soluble and viscous in

neutral (pH=7.0) or alkaline conditions (pH>7.0) (Jonas and others 1976).

27

V. Challenges in Raw Meat Manufacturing of Added Water Meat Products.

Raw Meat Quality

Meat processors have tried to select high quality raw materials to create a quality
ﬁnal product. Lower value meat cuts are those that possess marginal to poor quality
(Miller 2000). These cuts are likely to be inconsistent in color, lack tenderness and
juiciness. Pale, soft, and exudative (PSE) pork and DFD beef are two examples of lower
quality raw materials. Pale, soft, and exudative pork is soft in texture, paler in color and
wetter on the meat surface due to poor water binding properties. Pale, soft, and exudative
pork is a stress related disorder (Motzer and others 1998) that affects 10-30% of all pork
carcasses (Miller 1989). The PSE condition occurs when postmortem glycolysis is rapid
while carcass temperature is still high (Miller 1989). This combination causes protein
denaturation which promotes poor water-holding ability, increased meat softness, purge,
and paler color (Trius and others 1994b). For example, restructured ham manufactured
with PSE pork demonstrated lower chill yield values, more expressible moisture, and
lighter color than normal and 50% normal and 50% PSE hams (Motzer and others 1998).
The PSE condition also results in tough and dry cooked products. On the other hand,
DFD meat is higher in pH (>6.2), darker in color, ﬁrmer in texture and possesses a drier
meat surface. Dark, ﬁrm and dry meat has a higher water holding capacity which is
beneﬁcial for high added water products but has an unacceptable raw meat appearance.
Dark, ﬁrm and dry pork is due to stress over a period of time which results in the
depletion of muscle glycogen (Pearson and Tauber 1984). The DF D condition also

affects processed meat quality. For example, the use of DFD meat in the canning

28

industry causes residual pinkness (Schmidt and Trout 1994). It also increases the
microbial spoilage due to the high meat pH and can create “glazy” bacon (Pearson and

Tauber 1984).

Manufacturing Technologies

Processing technologies such as comminution, addition of non-meat ingredients,
thermal processing, and packaging are used to improve product tenderness, juiciness, and
uniformity of color and texture. A key processing principle for manufacturing
restructured meat products is the binding and retention of added water. This may be
accomplished through the injection of brine solutions into pieces or by direct addition to
the meat pieces in a tumbler or mixer. In the restructuring process, products are made
from muscle groups that are partially or completely comminuted and reformed to
resemble whole muscle. Restructuring uses three basic concepts: chunking and forming,
ﬂaking and forming; and tearing and forming (Pearson and others 1996). Restructuring
allows for portion control, easier slicing, and more accurate predictions of cock yields
(Pearson and Tauber 1984). However, the restructuring process does create problems
with color instability and lipid oxidation. Akamittah and others (1990) found that color
stability and lipid oxidation are highly correlated. Further research also showed that lipid
oxidation could be inhibited in restructured beef, pork, and turkey steaks for 4, 6, and
eight weeks respectively with the use of phosphate and salt at 0.3% and 1.5%.
Additionally, the restructuring process is a time consuming application that requires
additional machinery and labor. It allows for microorganisms to enter the meat while

being further processed and a decrease in shelf-life due to microbial growth.

29

Color

Several quality problems and challenges are encountered in added water
restructured meat products. The most serious of these problems are color instability and
fat oxidation (Akamittath and others 1990). The color of meat products is a prime factor
by which consumers judge their acceptability and product selection (Secrist 1982; Chen
and Trout 1991). It has been shown that the addition of water dilutes the concentration of
myoglobin, (Miller 2000) which results in a paler product color. Results suggest meat
discoloration and lipid oxidation are directly correlated in a study conducted on
restructured beef, pork and turkey restructured steaks (Akamittath and others 1990). In
addition, the use of lower quality meat cuts (PSE, DF D) can also affect the ﬁnal product
color and consistency. The use of BF D meat in cured meat products increases color
variability when used with normal and PSE meat. Restructured ham manufactured with
PSE pork demonstrated signiﬁcantly (P<0.05) lower cook yield values, more expressible

moisture, and lighter color (Motzer and others 1998).

Binding Ability

Meat binding ability refers to the ability of meat to hold fat and added water
during processing (Aberle and others 2001). The restructuring process must reassemble
and bind the ground, chopped, or sectioned meat together to form a product that
resembles a whole muscle upon cooking (Lin and others 1990). The addition of non-
meat ingredients such as SP1 and KC can increase meat binding ability. However, the
key component for successful restructured meat binding is protein extraction.

Mechanical processing procedures such as tumbling, massaging, and mixing can enhance

30

meat protein extraction. For example, tumbling sectioned and formed ham can aid in the
migration of cure and increase the extraction of salt soluble proteins, thereby increasing
the binding ability (Krause and others 1978; Ockerman and Organisciak 1978). The
extraction of salt soluble proteins during tumbling forms a sticky, protein exudate which
coats the surface of meat pieces and allows for binding pieces of meat together.
Furthermore, tumbling/massaging/mixing promotes the cohesion of meat pieces,
enhances tenderness, juiciness, increases cook yields and improves Sliceability.
However, determining the adequate time to mechanically extract protein can be difﬁcult
and cost ineffective initially to the meat processor. Mixing too much or too little will
result in an overly bound or poorly bound and an undesirable product (Lin and others
1990; Osbum 2001). Determining the adequate mixing/tumbling time can require
statistical modeling, researching competitor mechanical agitation times, or even a trial

and error process.

Product Texture

Although the use of non-meat ingredients such as phosphate, salt, SPI, modiﬁed
food starch (MFS), KC, and SC have been shown to improve product sensory
characteristics such as tenderness and juiciness (Schwartz and Mandigo 1976; Siegel and
others 1979; Smith and others 1984; Megard and others 1985; Jones and others 1987;
Alvarez and others 1990; Troutt and others 1992; Ahn and others 1999), restructured
meat products may exhibit soft and mushy texture after thermal processing. The addition
of water creates meat protein dilution resulting in a softer textured ﬁnished product

(Claus and others 1989). Soft texture and poor product appearance in added water

31

restructured products is directly correlated to inadequate tumbling/massaging/mixing
time. Mechanically agitating the pieces for too little time will cause crumbly, soft texture
and agitating for too long will cause tough, rubbery texture (Lin and others 1990).
Turkey breasts with 70% added brine demonstrated watery and soft texture with poor

binding as the restructured pieces were easily torn apart (Bater and others 1992)

Thermal Processing Yields and Purge

High product cook yield values after thermal processing are a desirable attribute
to the meat processor from an economical standpoint. However, conventional brine
solutions (salt, phosphate, cure) are still used. These “traditional” brine solutions are
providing the meat processor with lower cook yield values when compared to products
manufactured with additional non-meat ingredients. Acton (1983) found that a traditional
brine solution diluted protein exudates and resulted in decreased cook yields. The
addition of high amounts of water to decrease product costs has also increased released
ﬂuid or purge in the storage package. Purge is the loss of water during storage, which is
mostly seen in the product’s package at the retail case. This results in reduced consumer
appeal. The addition of non-meat ingredients such as KC, SP1, and MFS can improve
cook yield values and decrease purge loss. For example, the use of SPI can increase cook
yields by 30% in restructured, combination meat products (Siegel and others 1979).
Kappa carrageenan was shown to improve water retention in cooked pork sausage
(DeFreitas and others 1997). Modiﬁed food starch has been shown to decrease cook loss
values in low-fat ground beef patties (T routt and others 1992). Finally, Van den Hoven

(1987) discussed the abilities of SC for water retention and purge control.

32

VI. Approved Pugge Controllers for Meat Products.

Purge controllers approved by the USDA-FSIS have made it possible for meat
processors to increase product yields and decrease processing costs. There are four
approved purge controllers for ham products: carrageenan, SPI, MFS, and SC. These
ingredients each allow for increased water retention and textural enhancement of water-
added, restructured meat products. In addition, they also have the ability to increase

product shelf-life, binding ability, and nutritional value.

Carrageenan

The addition of KC to restructured and whole muscle meat products has resulted
in increased water binding and retention. For example, restructured turkey breasts
manufactured with 70% added water and 0.5% KC had 19% higher cook yield values
than the control (Bater and others 1992). Prabhu and Sebranek (1997) also demonstrated
higher cook yields and lower purge values in hams with 1.5% KC when compared to the
control. Additionally, a study utilizing 0.5% KC and/or 0.5% LC in beaker sausage
demonstrated lower cook loss values when compared to the controls (Trius and others
1994a).

In a study comparing the three major types (KC, IC, and LC) of carrageenan IC
was the most effective at increasing force-to-fracture, true shear strain, and water holding
ability (Foegeding and Ramsey 1987). KC is more effective than IC in increasing
hardness and equivalent to IC in true shear stress (F oegeding and Ramsey 1987). Kappa
carrageenan and IC also improved moisture retention of cooked pork sausage (DeFreitas

and others 1997). Kappa carrageenan effectively decreased freeze-and—thaw purge of

33

cured turkey thigh meat (Bater and others 1993). A combination of LC and KC] was
shown to decrease cooking loss of bologna (Trius and others 1994a). Lambda
carrageenan has the softest texture among the three major types of carrageenan. For
example, a bologna meat batter with LC was more viscous, yet the cooked product was
softer in texture exposing LC’s inability to create a ﬁrm gelling matrix (Trius and others
1994a). A decrease in beaker sausage ﬁrmness with LC was also seen in a study that
compared LC, KC, and IC conducted by Trius and others (1994a). In conclusion, of the
three forms (IC, LC, and KC) of carrageenan used in meat products, KC is the
recommended form in restructured and processed products. Kappa carrageenan has been
shown in numerous studies to increase cook yields, decrease purge, increase product

ﬁrmness and meat binding.

Soy Protein Isolate

The addition of SPI results in better binding and improved texture of meat
products (Megard and others 1985; Alvarez and others 1990; Ahn and others 1999). Soy
protein isolate increases cook yield and enhances the binding of the meat pieces by
minimizing the effect of excess water on extracted myoﬁbrillar proteins (Siegel and
others 1979). Furthermore, SPI provides better fat retention and increased gelling ability
than other forms of soy proteins (Porcella and others 2001). It has been shown that SPI
also increases the emulsifying capacity and the emulsion stability (Schweiger 1974).

Soy protein isolate also affects textural attributes, speciﬁcally ﬁrmness,
tenderness, and ﬂavor. For example, increased ham injection levels increased sensory

panel scores for juiciness and tenderness (Siegel and others 1979). In another study,

34

utilizing restructured mechanically deboned chicken with 10% SP1 improved tenderness
when measured by Wamer-Bratzler shear and tensile strength (Alvarez and others 1990).
In contrast, increasing the level of injection of SPI in hams negatively affected overall
acceptability, textural appeal, and ﬂavor (Siegel and others 1979). Thus, proper injection

level and SP1 concentration level should be evaluated for ideal product quality.

Modiﬁed Food Starch

Starch has traditionally been used in meat products to improve quality and to
extend the more expensive meat fraction of the product (Skrede 1989). Modiﬁed food
starch gelatinizes when heated thereby binding relatively large amounts of water. In an
experiment conducted comparing ﬁve different types (potato ﬂour, modiﬁed potato
starch, wheat, corn and tapioca) of starches, potato ﬂour was rated the best suited starch
for a stuffed, fresh meat sausage followed by wheat, while tapioca was the least suited
(Skrede 1989). Modiﬁed food starch improved freeze/thaw stability of the sausage
(Wotton and Chaudhry 1979; Howlings 1980). The chemical changes in MF S structure,
including cross-binding by phosphorus groups and the masking of hydroxyl groups by
acetyl group's, strengthen the starch granule by reducing the afﬁnity between the starch
molecules. In a study conducted on low fat ground beef patties, potato starch in
conjtmction with other non-meat ingredients reduced cooking loss and scores for oily

mouth coating while increasing pattie cohesiveness (Troutt and others 1992).

Sodium Caseinate

35

Sodium caseinate increases water and fat binding (Keeton 2001) and is used
primarily as an emulsifying agent. Sodium caseinate has been used as stabilizer for pre-
emulsiﬁed fat in a reduced-fat frankfurter while helping maintain the desired texture that
can be lost when salt is reduced and water is added (Su and others 2000). Sodium
caseinate does not bind meat pieces well but still provides ﬁrmness and water holding
capacities (purge controlling) in meat products (Van den Hoven 1987). It allows for
increased cook yields and lower purge values. an important purge controlling attribute
when adding high (70-110%) amounts of water to meat formulations. Furthermore,
solubility and viscosity of SC were altered by addition of salts and increase in

temperature (Konstance and Strange 1991).

VII. Potential Pu|_~ge Controllers

To address consumer concerns with respect to diet/ health issues, the meat
processing industry has focused on fat reduction by substitution of fat with added water.
Replacement of fat with added water helps ensure a tender, juicy product. Hydrocolloid
gums function as water-binding agents in numerous food products (Glicksman 1969)
including restructured meat. They are plant derived carbohydrates that provide creamy,
slippery properties that are similar to fat (Pearson and Gillett 1996). Cellulose is the most
important natural polymer available through renewable sources. However, cellulose has
low solubility and therefore to extend its application, a number of cellulosic derivatives
have been developed (Hirren and others 1996). Two such derivatives created under these
conditions are MC and HPMC. Limited research is available that investigates the

incorporation of MC and/or HPMC in meat products. These non-meat ingredients may

36

increase product yields by improving water binding capacity while minimizing released

water in the form of purge during packaging and subsequent storage.

Methylcellulose

Methylcellulose is a water-soluble, cellulose ether formed by an alkali treatment
of cellulose and followed by a reaction with methylchloride (Grover 1982). It is used as
a binder, emulsiﬁer, stabilizer and thickener in a variety of food products. It thermally
gels and reverses upon cooling. For example, in an aqueous solution, MC gels when
heated to approximately 50°C and then reverts into a solution upon cooling below room
temperature (< 22°C) In addition, MC is used in both pharmaceutical and food
industries due to its ability to form excellent ﬁlms (Donahowe and Fennema 1993).
Currently, MC is only allowed up to 0.15% in meat and poultry products based on total
product weight (USDA 2001). It is a GRAS product that assists with binding and WHC
of a meat product.

In general, cellulose hydrocolloids are used to bind moisture in meat products.
However, early research indicated that MC had adverse effects on cook yields, cook loss,
and texture. For example, beef patties containing 1% MC or HPMC contained less
moisture when compared to patties with no additive (Hill and Prusa 1988). An increase
in moisture loss during cooking with the addition of MC (0.2%) was further conﬁrmed
with an investigation of lowfat frankfurters (F oegeding and Ramsey 1986). On the other
hand, in chicken patties with MC at 0.25% yielded a higher (P<0.05) cook yield
(75.58%) than that of the control (74.66%) (Steinke 2001). Increased cook yield values

may be obtained if MC were incorporated into hi gh-moisture restructured meat products.

37

Hydroxypropyl Methylcellulose

Hydroxypropyl methylcellulose is another water-soluble, thermally reversible,
cellulose derivative. It is a food additive and “may be safely used in food, except
standardized foods, as an emulsiﬁer, ﬁlm former, protective colloid, stabilizer,
suspending agent, or thickener, in accordance with good manufacturing practice” (FDA
2001). Unlike MC that forms a very ﬁrm gel, HPMC forms semi-ﬁnn to soft gels at
hotter temperatures (60-90°C) depending on type (E, F, K grade). Hydroxypropyl
methylcellulose has three different grades known as E, F, and K that are structurally the
same but differ in gelling temperature and viscosity. Grade E is the least viscous (15-
4,000 cPs) and has the lowest gelling temperature (<77°C) and grade K is the most
viscous (99-100,000 cPs) and has the highest gelling temperature (<85°C).
Hydroxypropyl methylcellulose has been mostly used to reduce fat content in ﬁied foods.
French fries dipped into a solution of HPMC prior to deep fat frying were less greasy
than normal french ﬂies. The addition of HPMC has successfully reduced oil losses
during cooking and decreased cooking oil costs (Grover 1986). In a recent study, HPMC
reduced the migration of acetic acid from marinated chicken products into frying oil, thus
reducing the tocopherol (Vitamin E) loss in peanut oil (Holownia and others 2001).
Thus, HPMC can apparently form a barrier at the surface of the product in high
temperature environments. This barrier forming ability could also serve to enhance
product juiciness. For example, beef patties containing 1.0% HPMC were evaluated by a
sensory panel to have increased patty juiciness and tenderness (Hill and Prusa 1988).

Furthermore, results proved that the addition of HPMC reduced drip loss and total cook

38

loss values than control patties. By HPMC forming a surface barrier upon heating it may
enable the processor to increase cook yields and decrease purge losses of meat products

that contain HPMC.

VIII. Summaﬂ of Literature

It is clear in today’s economy the meat processor must be a cost effective and
efficient force. To achieve such a feat meat processors must produce a consumer
appealing and acceptable product that has high yields. The use of approved non-meat
ingredients such as KC, SPI, MFS and SC has made the task of increasing product water
retention, binding and textural enhancement an easier job. United States Department of
Agriculture approved purge controllers (KC, MFS, SC, SPI) have allowed for the
addition of higher amounts of water in ham products. Additionally, these ingredients
have proved to positively affect sensory attributes and product consistency.

Although, the approved ham purge controllers KC, SPI, MFS, and SC are reliable,
easy to use, and proven to be cost effective the meat processing and scientiﬁc community
must look outside the “box” for other options. Methylcellulose and HPMC are two such
“new” options that may enable the meat processor to signiﬁcantly decrease non-meat
ingredient costs by the utilization of lower addition percentages with enhanced water
binding and retention abilities. Non-meat ingredients such as SP1 and MFS require
higher addition levels (1-2%) while MC and HPMC may achieve the same attributes at
signiﬁcantly lower levels (02-04%). This signiﬁcant decrease in purge controller

percentages will be cost effective for the meat processor. If MC and HMPC can prove

39

their purge controlling and textural enhancing abilities, it could result in a larger return

for the meat processor and innovative processed meat products.

40

CHAPTER 2

Materials and Methods
This chapter provides detailed descriptions, procedures, and processes utilized
during the research project. Due to the extent and depth of each study it was necessary
that chapter 2 be devoted to the materials and methods used. Study I focuses on the
functional characteristics of hydrocolloid gums in water and brine solutions and in a meat
model system. Study 11 investigates the effects of incorporating various hydrocolloid
brine solutions on the sensory. textural and quality attributes of a commercial high-

moisture (45%) ham product.

I. Study 1: Evaluation of methylcellulose and hydroxypropyl methylcellulose

in water and brine solutions.

Introduction

As the amount of added water (>45% addition) in restructured meat products
increases, the ability to retain water during thermal processing and minimize purge
during storage decreases (Prabhu and Sebranek 1997). In previous literature, it has
been shown that hydrocolloids can increase water binding and retention (Trudso 1985;
Foegeding and Ramsey 1987; Bater and others 1992; Trius and others 1994a; Prabhu
and Sebranek 1997). However, research investigating MC hydrocolloids as a potential
purge controller has been limited. Therefore, we investigated the functionality of MC,

HPMC, and KC in water and brine solutions and in a meat model system to determine

41

the feasibility of incorporating hydrocolloid brine solutions in a high-moisture
restructured ham product.

Study I was conducted in four experiments. Experiment I investigated the
functional properties of selected hydrocolloids in a water solution. Experiment 11
investigated the functionality of the hydrocolloids in a brine solution (water, salt,
phosphate as the primary ingredients). Experiment III incorporated various types and
levels of hydrocolloids in brine solutions in a meat model system to determine their
impact on textural and quality attributes. The results from Experiment III determined
which hydrocolloid brine solutions were feasible for commercial restructured ham
manufacture. Experiment IV incorporated a combination of hydrocolloids in a brine
solution within a meat model system to determine if any beneﬁcial effects were
observed with respect to increased water binding and retention during storage. The
experiments also validated protocols, hydrocolloid brine and product formulations and
narrowed the selection of hydrocolloid brine solutions to be used during pilot plant
manufacture of a commercial high-moisture restructured ham.

Figure 1: Study I Flow Diagram

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

Selected Exp 1: Exp 11: Hydrocolloid
hydrocolloid Hydrocolloid brine
ingredients water solutions solutions
Exp IV: Application of Exp 111:
selected hydrocolloid brine Hydrocolloid brine
solutions in a model meat solutions in a model
system meat system
Study 11

 

 

 

42

Experimental Design and Data Analysis

For Study 1, both Experiment I and II were designed as a 4 x 4 factorial treatment
arrangement with the main effects of hydrocolloid type (A4M=MC I; F 4M=HPMC I and
K4M= HPMC H; KC) and level of incorporation (0.2, 0.4, 0.6, 0.8%) in either a water or
brine solution. Experiment HI was designed as a 4 x 4 factorial arrangement of
treatments with main effects of hydrocolloid type (MC 1, HPMC I, HPMC H, KC) and
level of incorporation (0.2, 0.4, 0.6, 0.8%) in a brine solution incorporated in a meat
model system with an augmented control (no hydrocolloids) (n=17). Experiment IV was
deigned as a one-way analysis of variance with four hydrocolloid brine treatment
combinations and a control (no hydrocolloids) (n=5). The hydrocolloid solutions were
formulated for addition at 45% (wt/wt). The level of signiﬁcance for all statistical
analyses was determined at P<0.05 (SAS User’s Guide, Version 8.2. Cary, NC: SAS
Institute; 2002).
Hydrocolloid Ingredients

Methylcellulose and HPMC food gums under the commercial name
METHOCELTM (Dow Chemical Company, Midland, MI) are water soluble carbohydrate
gums made from a natural cellulose source. The molecular structure of MC and HPMC
both contain the backbone of cellulose but HPMC possesses hydroxypropyl and
methoxyl substitutions (Anonymous 2000). These molecular differences contribute to
differences in viscosities, gelation temperatures and gel ﬁrmness between MC and
HPMC. Methylcellulose I is of medium viscosity (4,000 cPs), hydrates below 13°C and

forms a ﬁrm gel at 50-55°C. Hydroxypropyl methylcellulose I (HPMC I) is of medium

viscosity (4,000 cPs), hydrates below 25°C, and forms a semi-ﬁrm gel at 62-68°C.

43

Finally, HPMC II is of medium viscosity (4,000 cPs), hydrates below 295°C, and forms

soft gels at 70-90°C.

Kappa carrageenan is a hydrocolloid composed of sulfated linear polysaccharide
units extracted from red seaweeds. It is a GRAS substance and is an approved food
additive. Due to its ability to be a strong gelling agent, KC can be used for meat
applications such as restructured ham. The selected KC for these research studies was

Gelcarin® ME 6910 (FMC BioPolymer, Princeton, NJ). Unlike METHOCELW, KC

hydrates upon heating (70°C) and then forms a stable gel upon cooling to <25°C.
Experiments H, 111 and IV included in the hydrocolloid brine solutions STP
(Briﬁsol 512, BK Giulini Corporation, Simi Valley, CA), food grade sugar, salt, sodium

nitrite and sodium erythorbate.

Manufacturing Process
A. Hydrocolloid Water and Brine Solution Manufacturing (Exp. [-1 V)

Hydrocolloid water (Exp. I) and hydrocolloid brine (Exp. 11) solutions (909 g)
were developed and formulated according to the procedures in Appendices l, 2 and 3.
The hydrocolloid ingredients were randomly selected and weighed out (0.2, 0.4, 0.6 or
0.8% of the total solution) and placed in 946.4 mL lidded glass jars (Fisher Scientiﬁc Co.,
Pittsburgh, PA.) with the appropriate amount of water or brine. The solutions were
mixed using a 4-blade mixing head: 2-blades perpendicular (2.5 cm across) to the shaft
and 2-blades parallel to the shaft (1.3 cm equidistant from shaft) attached to a drill (SKIL,
S-B Power Tool Co., Chicago, IL). Experiment IV investigated the functional properties

of hydrocolloid brine solutions containing two or more combinations of hydrocolloid

44

ingredients. All solutions were covered and stored overnight (approximately 12-16 hrs)
in a walk-in cooler (2—4°C). Upon completion of storage (12-16 hrs) required amounts of
sodium nitrite (J .T. Baker, Phillipsburg, NJ) to achieve 156 ppm sodium nitrite and 250
ppm sodium erythorbate (Butcher and Packer Supply Co., Detroit, M1) were added to the
hydrocolloid solutions and mixed.

B. Model Meat System Processing (Exp. III and I V)

Fresh pork semimembranosus (IMPS 402F) muscles were obtained from a local
meat company and delivered to MSU Meat Laboratory. Upon arrival, boxed hams were
placed into cooler 2-4°C and 10 kg of ham was randomly selected for each replication.
Randomly selected hams were removed of excess fat and the gracilis muscle. Hams were
weighed (7.7 kg) according to the appropriate product formulation for each replication
(n=3) and covered with SaranTM wrap. Processing of the entire lot fresh ham’s occurred
within one week of arrival.

Pork semimembranosus muscle was ground through a 0.9 cm plate twice utilizing
a Toledo chopper (Model- 5126, Toledo Scale Corp, Toledo, OH). Four hundred grams
of ﬁeshly ground ham and 180 grams of the designated treatment brine solution were
added to a Hobart Kitchen Aid mixer (Model K5-A, Hobart Corporation, Troy, OH) and
mixed for 3 min at speed setting 2. The mixer bowl and mixing attachment were
thoroughly washed and dried between each treatment formulation.

C. Thermal Processing

Thirty-four grams (in triplicate) of the designated hydrocolloid water (Exp. 1) or

brine (Exp. H) solutions were placed into 50 mL polycarbonate centrifuge tubes, capped

and then placed into a programmed water bath (Model 9510, PolyScience, Niles, IL) that

45

mimicked a restructured ham thermal processing schedule. Procedures on water bath

programming are given in Appendix 4.

Table l: Programmed Water Bath Schedule

 

 

Time Internal Bath Temperature
Stage (Min) Temp (°C) (°C)
1 30 0 4.0
2 15 0 43.3
3 3O 0 54.4
4 30 0 60.0
5 30 0 65.6
6 60 70.0 79.4
7 30 37.8 35.0

 

The samples were thermally processed to an internal temperature of 70°C. The same
procedures were followed for the manufacture of a high-moisture restructured ham in a
model system (Exp. 11 and IV). For analyses purposes thermally processed, restructured
ham was removed from polycarbonate test tubes resulting in a cylindrical, test tube

shaped ham sample (i.e. “plug”).

Analyses
A. pH determination

Determination of hydrocolloid water and brine solution pH values for all Study I
experiments were determined at 5°C using an Accumet pH Meter (AB 15, Fisher
Scientiﬁc, Co., Pittsburgh, PA) calibrated with phosphate buffers 4.0 and 7.0.
Restructured ham raw and cooked pH values (Exp. III and IV) were determined by
placing one gram of sample into a 50 mL centrifuge plastic tube and adding ten mL of
distilled, deionized water. Samples were homogenized with a Polytron mixer (PT-35,

Kinematica, AG, Switzerland) on speed setting 2 for two, 10 sec bursts. The pH of each

46

sample was measured in duplicate using an Accumet pH meter (AB 15, Fisher Scientiﬁc,
Co., Pittsburgh, PA) calibrated with phosphate buffers 4.0 and 7.0.
B. Viscosity Analysis in Hvdrocolloid Water and Brine Solutions
The viscosity readings of each hydrocolloid water and brine solution (909 g) were
measured in the 946.4 mL glass jars (Fisher Scientiﬁc Co., Pittsburgh, PA) using a
Brookﬁeld Viscometer (Model DV-II, Brookﬁeld Engineering, Co., Stoughton, MA) at
speed setting 12. A variety of spindle sizes were used due to differences in viscosity
between water and brine solution treatments. Spindle size 2 was used for hydrocolloid
water solution (Exp. I) viscosity readings while spindle size 3 was used to determine
hydrocolloid brine solution viscosity (Exp. H and HI). Spindle size 6 was used for the
multi-hydrocolloid brine solution treatments while spindle size 5 was used for the
control brine solution (Exp. IV). The selected spindle was lowered into the geometric
center of the water or brine solution until the indented ring on spindle was level with
solution surface. Viscosity readings were recorded in centipoise (cPs) once the
displayed reading was stabilized. Prior to viscosity analysis, the viscometer was
calibrated to assure accuracy. The detailed calibration procedure in Appendix 5.
C. Color Analysis
A ColorTec PCMTM Color Meter (Model 6482, ColorTec Associates, Clinton, NJ)
with a 10° standard observer and an 8 mm reading oriﬁce was used to measure the color
of thermally processed (70°C) hydrocolloid water and brine solution gels (Exp. I and H).
The ColorTec was programmed to analyze L* (lightness), a* (redness), b* (yellowness)
(Commission Internationale De L’Eclairage (CIE)), with D65 illuminant (daylight

illuminator), and calibrated on a standard white and black tile. Readings were taken on

47

the exposed exterior surface of the hydrocolloid water and brine solution gel plugs.
Additionally, in experiment HI and IV the same procedures were utilized to determine the
color (L*, a*, b*) values of the interior surface of thermally processed (70°C)
restructured ham "plugs" (thermally processed ham removed from polycarbonate tube;
i.e. plug) manufactured with various hydrocolloid brine solutions. Restructured ham
“plug” was cut longitudinally down the center of ham to form two equal halves for
interior surface color analysis. Three readings per ham sample were taken and averaged
for L* (lightness), a* (redness), and b* (yellowness) values.

D. Water Retention (Exp. I and 11)

Water binding and retention properties of thermally processed (70°C) hydrocolloid
water and brine solution gels were measured. Hydrocolloid water and brine solutions
(34g i 0.1g) containing MC or HPMC were placed in 50 mL polycarbonate centrifuge
tubes, thermally processed and removed from the water bath once the targeted 70°C
internal temperature was reached. Methylcellulose and HPMC gel upon thermal
processing and reverse upon cooling. Solutions containing MC or HPMC were removed
at 70°C to assure full gelation and accurate water retention values. Solutions containing
KC were removed after cooling to an internal temperature of 37.8°C. Kappa carrageenan
solutions were allowed to cool as KC gels upon cooling following thermal processing.
Solution temperatures were monitored utilizing three Omega thermocouples (Model
TMTSS-OZOG-6, Omega Engineering, Inc., Stamford, Conn.) inserted through the cap of
the polycarbonate tubes. The samples were removed, the tubes inverted to allow the
samples to drain into a funnel lined with cheese cloth, and allowed to drip for 1 min.

Sample exudate was collected below the funnel spout in a pre-weighed 15 mL graduated

48

cylinder for 1 minute, weighed and water retention values determined by the following
equation:
% water retention = Initigl solution wt.- Exudate wt. x 100
Initial solution wt.
E. Cooked Product Yield and 7-day Purge (Exp. III and IV)

Cooked product yield determinations for restructured hams manufactured in a model
system were performed after the ham "plugs" were thermally processed (70°C) and
cooled to an internal temperature of 37.8°C. The ham "plugs" were carefully released
from the interior surface of the tubes with a ﬂat spatula. The tubes were inverted and the
water released from the ham samples was ﬁltered through a funnel lined with cheese
cloth and collected in a pre-weighed 15 mL graduated cylinder for 1 min, the cylinder
reweighed and percent cook yield determined by the following equation:

% cook yield = Raw megt wt.- Exudate wt. x 100
Raw meat wt.

The polycarbonate centrifuge tube containing the remaining ham sample was recapped
and placed into 2-4°C cooler and chilled for 12-16 hours until an internal temperature of
4°C was reached. The chilled restructured ham plugs were then used for 7-day purge
analysis.

To determine percent purge, chilled restructured ham plugs were removed from
polycarbonate centrifuge tubes and the sample weight recorded. Each ham plug sample
was placed into 12.7 cm x 22.9 cm vacuum bags (Cryovac Sealed Air Corp., Duncan,
SC) and heat sealed using an impulse heat sealer (Diagger, Lincolnshire, IL). A non-
sterile 20 gauge needle attached to the 1.5 cm diameter rubber hose of a vacuum pump

(Welch Vacumn, Skokie, IL) was inserted into the sealed bag to extract air. Each bag

49

had a vacuum of 43 cm Hg pulled. After air extraction, the bag was heat sealed again to
prevent air from ﬂowing back into the bag from the needle insertion point. Packaged
restructured ham plugs were stored in a 2-4°C cooler for 7 days. On day 7, each sample
package was reweighed, the ham sample plugs removed, the ham sample and vacuum
bag blotted dry and both were reweighed. The percent purge loss was determined using
the following calculation:

% purge loss = Total pkggwt. - (Dry pkgwt + Drv meat m x 100

Total pkg. wt.
F. T extural Analysis
Gel Strength/Hardness (Exp. 1 and II)

The gel strength/hardness of thermally processed hydrocolloid water and brine
solutions was analyzed on a TA-I-IDi texture analyzer (Texture Technologies
Corporation, Scarsdale, NY) utilizing a 5 kg load cell and a 1.3 cm diameter acrylic
cylinder attachment (TA-10) 3.5 cm in height. Each hydrocolloid water and brine
solution gel plug was analyzed in the 50 mL centrifuge tubes in which they were
thermally processed. The MC and HPMC solutions were analyzed at 70°C and the KC
solution was analyzed at 378°C to assure measurements recorded on fully gelled
hydrocolloid solutions. Sample tubes were placed in a molded steel pipe ﬁtting placed on
the heavy duty platform (TA-90) to eliminate tube movement and variability during the
analysis. The acrylic probe penetrated the gel plug in the geometric center of the sample,
depressing the gel 8 mm before retracting. Peak force was recorded in grams with a

cross-head speed of 1.7 mm/s. Detailed gel hardness/strength settings for the TA-HDi

50

Textural Analyzer (Texture Technologies Corporation, Scarsdale, NY) are provided in
Appendix 6. Detailed protocol for calibration procedures can be seen in Appendix 17.
G. Texture Proﬁle Analysis (T PA) :2-cycle Compression (Exp. [11 and [W

Experiment HI and IV restructured ham test tube plugs were analyzed using the 2-
cycle compression test method, utilizing a TA-HDi Textural Analyzer (Texture
Technologies Corporation, Scarsdale, NY). Two restructured ham samples per treatment
were removed from the test tubes, covered to prevent surface drying and kept at 4°C.
Two circular samples measuring 2.5 cm (dia) x 2.5 cm (height) were cut horizontally
from the center of each ham plug using a size 11, non-sterile surgical blade attached to a
scalpel. Treatments were analyzed in duplicate. Each sample was weighed and analyzed.
A 5 kg load cell was used to measure hardness, springiness, cohesiveness, chewiness, and
resilience using a 75 mm diameter aluminum cylinder plate (TA-30), on a heavy duty
platform~ (TA-90). Samples were compressed to 25% of their original height (75%
compression) in a 2-cycle compression at 4-6°C with a crosshead speed of 1.7 mm/s. See
Appendix 7 for detailed TA-HDi Textural Analyzer (Texture Technologies Corporation,

Scarsdale, NY) settings and Appendix 17 for calibration procedures.

II. Study II- Evaluation of meth ylcellulose, hydroxypropyl methylcellulose and

kappa carrageenan in high-moisture restructured hams.

Preliminary Studv

51

A preliminary study was conducted to conﬁrm Study I results. The hydrocolloid
brine solutions from experiment IV were evaluated in addition to three control brine
solutions. Hydrocolloid brine solutions formulated:

Treatment 1 — 0.4% MC I x 0.6% HPMC 1

Treatment 2 — 0.4 % MC I x 0.6% KC

Treatment 3 — 0.6% HPMC Ix 0.6% KC

Treatment 4 — 0.4% MC I x 0.6% HPMC Ix 0.6% KC

Treatment 5 - Control

Treatment 6 - 0.4% MC I

Treatment 7 —- 0.6% HPMC I

Treatment 8 — 0.6% KC
This preliminary study veriﬁed protocols and procedures to insure consistent processing
for the manufacture of high-moisture restructured hams. Treatment brine solutions were
mixed using a Rotostat mixer (Model 80XP63SS, Admix Inc., Londonderry, NH)
modiﬁed by Michigan State University at 1200 rpm during the addition of phosphate,
salt, and sugar. During the addition of the hydrocolloid gums mixing speed was
increased to 1500 rpm to fully entrain hydrocolloid. Total mixing time was 20 minutes
per brine. The brines were covered and placed in a 2°C cooler for 12-16 hrs. Upon
completion of storage (12-16 hrs), brines were remixed for 1 minute at 1200 rpm. Nitrite
and erythorbate were then added and mixed for an additional 2 minutes at 1200 rpm.
Fresh pork semimembranosus muscle (gracilis muscle removed) was sorted in 5.7 kg
batches per restructured ham treatment. The ham muscles were further divided into three

1.9 kg batches for grinding into three different particle sizes (TORREY Grinder Model

52

M-32-5, Maquinas Para Mercados, S.A. DE C.V., Mexico). The ground ham muscles
(5.7 kg, 1.9 kg of each particle size) and 2.6 kg of either a hydrocolloid or control brine
(45% addition) solution was placed into a modiﬁed double axle paddle mixer (Model T-
268, Keebler Engineering Inc., Chicago, IL) and mixed for 10 min at mixer speed setting
1. Mixed restructured ham batter was placed into a vacuum stuffer (Model 500,
VEMAG Maschinenbau GmbH, Germany), stuffed into a pre-soaked ﬁbrous, non-
perforated, preclipped casings (Devro-Teepak, Inc., Kansas City, MO.), and clipped
using a Tipper Tie Clipper (Model PR465L, Dover Industries Co., Apex, NC). Thermal
processing was achieved utilizing a one truck smokehouse (CGI Processing, Model A28-
BOlOl, Automated Manufacturing, Cicero, IL). A processing schedule was established
during the process. Thermally processed, restructured hams were placed into a 2-4°C
cooked meat cooler and chilled for approximately 16 hours. All restructured ham
treatments were evaluated for casing peelability, ﬁrmness and Sliceability. Restructured
ham formulations that exhibited poor Sliceability and/or soft texture were eliminated from
ﬁirther investigation. Acceptable restructured ham treatments were 2, 3, 4, 5, and 8.
These hams were sliced (1.27 cm), vacuum packaged and stored (2°C) for sensory panel
training. Unacceptable restructured hams treatments were 1, 6, and 7. These hams were
disposed of properly as they exhibited poor peelability, Sliceability, soft in texture, and

low cook yields.
Experimental Design and Data Analysis

The experimental design was a one way AN OVA with three treatment

combinations (0.4% MC I/0.6% KC, 0.6% I-[PMC I/0.6% KC, 0.4% MC I/0.6% HPMC

53

I/0.6% KC) at 45% addition (wt/wt), with a hydrocolloid brine control (KC at 0.6 %;
45% addition wt/wt) and a control (no hydrocolloid; 45% addition, wt/wt). Main effect
means were separated by Tukey's Honest Signiﬁcant Difference test with a
predetermined level of P<0.05 (SAS User’s Guide, Version 8.2. Cary, NC: SAS Institute;
2002). The study was replicated three times.
Hvdrocolloid Ingredients
The hydrocolloid ingredients were described previously in Study 1.
Manufacturing Process
A. Brine Manufacturing
Three multi-hydrocolloid, a KC, and a control (n=5) brine solutions were
prepared for each replication for each treatment group on three consecutive days. Each
brine solution was randomly selected and formulated prior to each restructured ham
production day. The formulated treatment brine solutions were:
Treatment 1 - 0.4% MC Ix 0.6% KC
Treatment 2 — 0.6% HPMC Ix 0.6% KC
Treatment 3 — 0.4% MC I x 0.6% HPMC Ix 0.6% KC
Treatment 4 -— Control
Treatment 5 - 0.6% KC
Treatment brine solutions weighing approximately 11.3 kg each were placed in
plastic containers and mixed using Rotostat mixer (Model 80XP63SS, Admix Inc.,
Londonderry, NH) at 1200 rpm during the addition of phosphate, salt, and sugar. During
the addition of the hydrocolloid gums mixing speed was increased to 1500 rpm to fully

entrain hydrocolloid. Total mixing time was 20 minutes per brine. The brines were

54

covered and placed in a 2°C cooler for 12-16 hrs. Upon completion of 12-16 hrs storage,
brines were remixed for 1 minute at 1200 rpm. Nitrite and erythorbate were then added
and mixed for an additional 2 minutes at 1200 rpm.

B. Restructured Ham Processing

Approximately 136.1 kg of fresh, boneless, semimembranosus muscle (IMPS
402F), with the gracilis muscle on, were acquired from a local meat company and
delivered to MSU Meat Laboratory. Upon arrival, the hams were placed into a cooler (2-
4°C). Ham muscles were randomly selected and trimmed to remove the gracilis muscle
and external fat. The ham muscles were weighed out according to the appropriate
product formulation, placed in plastic meat lugs and covered with SaranTM wrap. The
time from ham muscle procurement to commercial restructured ham manufacture of all
three replications was one week.

Approximately 29.6 kg of fresh pork semimembranosus muscle (gracilis muscle
removed) was sorted in 5.7 kg batches per restructured ham treatment. The ham muscles
were further divided into three 1.9 kg batches for grinding into three different particle
sizes (Prabhu and Sebranek 1997). One 1.9 kg batch was ground through a 5.33 cm plate
(kidney plate), the second batch was ground through 2.54 cm plate and the last batch was
ground through a 0.95 cm plate (TORREY Grinder Model M-32-5, Maquinas Para
Mercados, S.A. DE C.V., Mexico). The ground ham muscles (5.7 kg, 1.9 kg of each
particle size) and 2.6 kg of either a hydrocolloid or control brine (45% addition) solution
was placed into a modiﬁed double axle paddle mixer (Model T—268, Keebler Engineering
Inc., Chicago, IL) and mixed for 10 min at mixer speed setting 1. Upon completion of

mixing, a sample for raw proximate analysis and pH determination were collected and

55

placed into labeled whirl-pak bags. Mixed restructured ham batter was placed into a
vacuum stuffer (Model 500, VEMAG Maschinenbau GmbH, Germany), stuffed into a
pre-soaked 11.4 cm x 76.2 ﬁbrous, non-perforated, preclipped casing (Devro-Teepak,
Inc., Kansas City, MO.), and clipped using a Tipper Tie Clipper (Model PR465L, Dover
Industries Co., Apex, NC). Stuffed and clipped ham chubs were weighed and recorded as
a treatment group. Each chub weighed approximately 2.3 kg with 3 chubs per treatment
group, 6.9 kg per treatment (15 restructured ham chubs per replication). Restructured
ham chubs were labeled, hung on smoke sticks, and placed on a smoke truck for thermal
processing.
C. Thermal Processing

Thermal processing was achieved utilizing a one truck smokehouse (CGI
Processing, Model A28- B0101, Automated Manufacturing, Cicero, IL) and processed
according the following smokehouse schedule:

Table 2: Smokehouse Schedule

 

 

Time Internal Dry Bulb Wet Bulb

Stage (Min) (°C) Smoke (°C) (°C) Fan Damper

1 15 0 No 43.3 3 7.8 50 Open

2 30 0 No 54.4 43.3 50 Open

3 30 0 No 60.0 46.1 50 Open

4 3O 0 No 65.6 48.9 50 Open

5 45 62.8 No 71.1 54.4 50 Open

6 120 62.8 No 71.1 62.8 50 Open

7 240 70.0 Steam 79.4 71 . 1 50 Open
Shower 30 54.4 No 1 min on 1 min off 100 Closed

 

Following the shower cycle, the restructured hams were removed from
smokehouse once an internal product temperature of 54.4°C was reached. The
restructured hams were allowed to equilibrate to an internal temperature of 378°C (30

min) at 20°C. Excess water was removed and the treated products weighed to determine

56

product cook yields (3 78°C). The restructured hams were then allowed to equilibrate to
an internal temperature of 322°C (15 min) at 20°C prior to chilling. The hams were

placed into a 2-4°C cooked meat cooler and were chilled to 4°C according to Appendix B
guidelines (USDA-FSIS).
D. Chilling, Slicing, and Packaging Process

Thermally processed restructured hams were placed into a 2-4°C cooked meat
cooler and chilled for approximately 16 hours. Casings were then removed from hams
and discarded.

Three restructured ham chubs per treatment were sliced into 1.27 cm thick slices
using a Globe meat slicer (Model 775L, Mozley Mfg. Co. Inc., Stamford, CN) and placed
on plastic trays according to treatment. Restructured ham slices were randomly selected
and vacuum packaged. Two slices were utilized for cooked proximate composition and
pH determination; chopped into 1 cm pieces, placed in whirl-pak bags, sealed, labeled
and stored in a -28.8°C freezer. Twelve randomly selected ham slices were packaged for
trained sensory panel evaluation and packaged into two (6 slices per bag) 30.5 cm x 35.6
cm vacuum package bags (Cryovac Sealed Air Corp., Duncan, SC). One ham slice was
randomly selected for day 0 lipid oxidation analysis, packaged in a 12.7 cm x 22.9 cm
bag and sealed with no vacuum using an impulse heat sealer (Diagger, Lincolnshire, IL).
Four ham slices were randomly selected for textural analysis - two for objective texture
proﬁle analysis and two slices for Kramer Shear analysis. These slices were packaged in
17.8 cm x 30.5 cm vacuum package bags. Twenty ham slices were randomly selected for
color, purge, and lipid oxidation analyses; 4 slices per day, 2 slices per bag (17.8 cm x

30.5 cm), 2 bags per treatment for evaluation on day 7, 14, 21, 28, and day 56 of

57

refrigerated (4°C) storage. Extra ham slices packaged in 30.5 cm x 35.6 cm vacuum
package bags. All vacuum packaged samples were packaged using a Multivac vacuum
packager (AGW, SeppHaggenmuller KG, Germany) with a vacuum setting of 2.5
vacuum and a heat sealer bar setting of 3.0.
Restructured Ham Storage

Vacuum packaged restructured ham slices were placed in a 4°C 1- 1°C, walk-in
cooler. Packages were laid ﬂat, non-overlapping on white trays which were placed on
tables 2.08 meters from a constant light source. The cooler contained 10 lighting ﬁxtures
and 2 ﬂuorescent lamps (Model F4OSP41, General Electric, Cleveland, OH) per ﬁxture
(n=20). Lighting was monitored everyday for a total of 56 days, lamps were changed as
needed and never turned off. F oot-candle (F C) readings (F C=80) were taken using a GE
Triple Range Light Meter (Model 217, General Electric, Cleveland, OH) from the surface
of the ham slice. The light meter was set in the middle range (FC=50-250). The foot-

candle reading (F C =80) is equivalent to 24,407 lumens (Appendix 10).

Analyses
A. Hydrocolloid Brine solution and product pH Determination
Brine solution and raw and cooked restructured ham pH values analyses were
determined as previously described in Study 1.
B. Product Cook Y ielwetermination
Cooked product yield was determined as previously described in Study 1.
Detailed procedure for cook yield can be found in Appendix 11.

C. Color Analysis, TBARS analysis and Purge loss

58

Objective color determinations for the exterior ham surface (exposed to light) and
the interior ham surface (unexposed to light) was measured using a Minolta Chromameter
(Model CR-310, Minolta Camera Co., Ramsey, NJ). Three readings were taken and
averaged for L* (lightness), a* (redness), and b* (yellowness) values (Commission
Internationale De L’Eclairage) (CIE). The Chromameter was set on D65 illuminant
(daylight illuminator), 2° standard observer, with a 50 mm reading oriﬁce. The
Chromameter was calibrated on a standard white and the pink color tile. Color readings
were taken for day 0, 7, 14, 21, and 28.

Thiobarbituric acid reactive substances (TBARS) analysis was conducted on day
0, 14, 28, and day 56, to monitor oxidative rancidity. Day 14 was the day the trained
sensory panel evaluated the corresponding samples. Four replicates were run for each
sample according to methods established by Tarladgis and others (1960) and Zipser and
others (1962) as modiﬁed by Rhee (1978) (Appendix 12). Percent purge was determined
for days 7, 14, 21, 28, and day 56 of refrigerated (4°C storage) as previously described in
Study 1.

Proximate Composition

Moisture (oven drying), fat (Soxhlet ether extraction), and protein (nitrogen
measurement, Model FP-2000, LECO Co., St. Joseph, M0) were determined according
to AOAC (2000) methods found in Appendix 8. Samples were analyzed in triplicate.
T extural Analyses

A. Texture Proﬁle Analysis (T PA) :2-cycle Compression
Restructured ham slices were analyzed using the 2-cycle compression test

method, utilizing a TA-I-IDi Texture Analyzer (Texture Technologies Corporation,

59

Objective color determinations for the exterior ham surface (exposed to light) and
the interior ham surface (unexposed to light) was measured using a Minolta Chromameter
(Model CR—310, Minolta Camera Co., Ramsey, NJ). Three readings were taken and
averaged for L* (lightness), a* (redness), and b* (yellowness) values (Commission
Internationale De L’Eclairage) (CIE). The Chromameter was set on D65 illuminant
(daylight illuminator), 2° standard observer, with a 50 mm reading oriﬁce. The
Chromameter was calibrated on a standard white and the pink color tile. Color readings
were taken for day 0, 7, 14, 21, and 28.

Thiobarbituric acid reactive substances (TBARS) analysis was conducted on day
0, 14, 28, and day 56, to monitor oxidative rancidity. Day 14 was the day the trained
sensory panel evaluated the corresponding samples. Four replicates were run for each
sample according to methods established by Tarladgis and others (1960) and Zipser and
others (1962) as modiﬁed by Rhee (1978) (Appendix 12). Percent purge was determined
for days 7, 14, 21, 28, and day 56 of refrigerated (4°C storage) as previously described in
Study 1.

Proximate Composition

Moisture (oven drying), fat (Soxhlet ether extraction), and protein (nitrogen
measurement, Model FP-2000, LECO Co., St. Joseph, M0) were determined according
to AOAC (2000) methods found in Appendix 8. Samples were analyzed in triplicate.
T extural Analyses

A. Texture Proﬁle Analysis (T PA ) :2-cycle Compression
Restructured ham slices were analyzed using the 2-cycle compression test

method, utilizing a TA-I-IDi Texture Analyzer (Texture Technologies Corporation,

59

Scarsdale, NY). Texture proﬁle analysis was conducted in conjunction with trained
sensory panel analysis on day 14. Two restructured ham slices per treatment (n=10) were
removed from vacuum packaged bags and held at 4°C. Two circular samples 1.9 cm
diameter x 1.3 cm thick, were cut from the center from each ham slice using a #12
stainless steel hand corer. Quadruplicate sample were analyzed for each restructured ham
treatment (n=60). A 5 kg load cell was used to measure hardness, springiness,
cohesiveness, chewiness, and resilience using a 75 mm diameter aluminum cylinder plate
(TA-30), on a heavy duty platform (TA-90). Samples were compressed to 25% of
original height (75% compression) in a 2-cycle compression at 4—6°C with a crosshead
speed of 1.7 mm/s. Appendix 13 describes the TA-HDi Texture Analyzer (Texture
Technologies Corporation, Scarsdale, NY) settings and Appendix 17 has calibration
procedures.
B. Kramer Shear F orce Determination

Restructured ham slices were analyzed using the Kramer S-blade shear force test
method, utilizing a TA-I-IDi Texture Analyzer (Texture Technologies Corporation,
Scarsdale, NY). Shear force analysis was conducted in conjunction with trained sensory

panel analysis on day 14. Two restructured ham slices (4—6°C) per treatment were

removed from vacuum packaging and covered to prevent surface drying at 4°C. A
rectangular sample measuring 7.9 cm x 6.4 cm x 1.3 cm was cut from the center of each
ham slice using a pre-made plastic template. A 50 kg load cell with a crosshead speed of
1.7 mm/s was used to measure peak force in Newtons (N) required to shear the
restructured ham slice. The 5-blade shear attachment was applied perpendicularly to the

sample. The blades were set to completely shear through ham sample. The peak force

60

required to shear through the restructured ham slice was reported in force per unit mass
of sample (N/g). Appendix 14 describes the TA-HDi Texture Analyzer (Texture
Technologies Corporation, Scarsdale, NY) settings for Kramer shear force analysis.

Additionally, Appendix 17 describes detailed calibration procedures.

Trained Sensory Panel Evaluation

A trained sensory panel was utilized to determine speciﬁc sensory attributes of
each restructured ham product. The panel was trained according to AMSA (1995) and
Meilgaard and others (1991). Each restructured ham treatment was evaluated using an 8
point hedonic scale, where 1=extremely soft and 8=extremely hard, 1=extremely dry and
8=extremely juicy, l=no residue/mouth coating and 8=abundant residue/mouth coating,
l=no off-ﬂavor detected and 8=abundant off-ﬂavor. An example of the trained sensory
ballot is found in Appendix 15. Restructured ham slices were stored at 4°C and
evaluated after l4 days of refrigerator storage. Samples were transferred to the Michigan
State University sensory testing facility and placed in a 4°C cooling unit. Samples were
prepared by cutting 1.27 cm3 cubes from the center portion of each ham slice and were
served cold (4-6°C). To minimize positional bias, the order of sample preparation was
randomized within each session (Meilgaard and others 1991).

Testing took place in climate controlled, partitioned booths with cool
incandescent light. Three cubes were placed in a plastic custard dish and held, covered to
prevent surface drying in a 4°C cooling unit until serving. Each sample was served to
panelists through a vertical sliding door that separated the food preparation area from the

sensory testing area. Panelists were instructed to handle sample cubes with supplied

61

wooden toothpicks, and tasted for hardness, juiciness, residue/mouth coating, and off-
ﬂavor intensity. Expectorant cups were provided to prevent taste fatigue as the panelists
were instructed not to swallow the samples. Distilled, deionized water and unsalted soda
crackers were used to clean the palate between samples. Fifteen (4 treatments, 1 control
and 3 replications) samples were evaluated in one day. The day was divided into 3
sessions with 5 samples evaluated per session. The panelists were standardized for each
session by evaluating l warm-up sample and discussing the results. The warm-up
samples were either the control or the KC treatment. There was 5 minutes between each
sample and a 15 minute break between sessions. The serving order was randomized by

treatment and replication (Appendix 16).

62

References

Aberle, ED, Forest, J C, Gerrard, DE, Mills, EW. 2001. Principles of Meat Science, 4th
Ed. CO: Kendall/Hunt Publishing. P 109-153.

Acton, J C. 1983. The Basic Concept of Restructuring. In: Carpenter, JA, editor.
Proceedings: 25‘h Annual Meat Science Institute. Athens, GA: University of Georgia,
Food Science Department. P 1-9.

Acton, J C, Dick, RL. 1984. Protein-protein interaction in processed meats. Reciprocal
Meats Conference Proceedings 37:36.

Adams, JR, Huffman, DL. 1972. Effect of controlled gas atmosphere and temperature on
quality of packaged pork. J Food Sci 37:869-872.

Ahn, H, Hsieh, F, Clarke, AD, Huff, HE. 1999. Extrusion for producing low-fat
pork and its use in sausage as affected by soy protein isolate. J Food Sci 64(2):267-27l.

Akamittah, JG, Brekke, CJ, Schanus, EG. 1990. Lipid oxidation and color stability in
restructured meat systems during frozen storage. J Food Sci 55(6):1513-1517.

Alvarez, VB, Smith, DM, Morgan, RG, Booren, AM. 1990. Restructuring of
mechanically deboned chicken and non-meat binders in a twin-screw extruder. J Food Sci
55:942-946.

AMSA. 1995. Research guidelines for cookery, sensory evaluation, and instrumental
measurements of fresh meat. American Meat Science Association and National Livestock
and Meat Board, Chicago, IL.

Anonymous. 2000. Product selection guide for METHOCEL food gums. The Dow
Chemical Company.

Anonymous. 2001. A food technologist's guide to METHOCEL food gums. The Dow
Chemical Company.

Anonymous. 2003. Non-meat ingredients, seasonings, and spices. Value-Added Meat
and Poultry School. Texas A&M University, January 2003.

AOAC. 2000. Meat and meat products. In: Cunniff, P, editor. Official methods of
analysis of AOAC International. Washington, DC: AOAC International. P 1-23.

Areas, JAG, Lawrie, RA. 1984. Effect of lipid-protein interactions on extrusion of offal
protein isolates. Meat Sci 11:275-299.

63

Asghar, A, Samejima, K, Yasui, T. 1985. Functionality of muscle proteins in gelation
mechanisms of structured meat products. CRC Critical Review. Food Sci Nutr 22:27.

Bailey, AJ. 1984. The chemistry of intramolecular collagen. In: Bailey, AJ, editor. Recent
Advances in the Chemistry of Meat. London: Royal Soc. Chemistry

Barbut, S, Maurer, AJ, Lindsay, RC. 1988. Effects of reduced sodium chloride and added
phosphates on physical and sensory properties of turkey frankfurters. J Food Sci
53(1):62-66.

Barbut, S, Mittal, GS. 1988. Rheological and gelation properties of meat batters prepared
with three chloride salts. J Food Sci 53(5): 1296-1299,13l l.

Bater, B, Descamps, O, Maurer, AJ. 1992. Quality characteristics of hydrocolloid-added
oven-roasted turkey breasts. J Food Sci 57: 1068-1070.

Bater, B, Descamps, O, Maurer, AJ. 1993. Quality of characteristics of cured turkey
thigh meat with added hydrocolloids. J Poult Sci 72:349-3 54.

Belton, PS, Packer, KJ. Southon, TE. 1987. C1 nuclear magnetic resonance studies of the
interaction of chloride ions with meat in the presence of tripolyphosphate. J Sci Food
Agric 40:267-275.

Berry, BW, Smith, J], Secrist, JL, Douglass, LA. 1988. Consmner response to
restructured beef steaks processed to have varying levels of connective tissue. J Food
Qua] 11:15-25.

Boles, JA, Parrish, F C. 1990. Sensory and chemical characteristics of precooked
microwave-reheatable pork roasts. J Food Sci 55(3):618-620.

Booren, AM, Jones, KW, Mandingo, RW, Olson DG. 1981. Effects of blade
tenderization, vacuum mixing, salt addition and mixing time on blending of meat pieces
into sectioned and formed beef steaks. J Food Sci 46:1678-1680.

Borisova, MA, Oreshkin, EF. 1992. On the water condition in pork meat. Meat
Sci 31:257-265.

Boume, CB. 1982. Food texture and viscosity: concept and measurement. New York,
NY: Academic Press.

Cassidy, RD, Ockerman, HW, Krol, B, VanRoon, PS, Plirnpton, RF Jr, Cahill, VR
1978. Effect of tumbling method, phosphate level, and ﬁnal cook temperature on the
histological characteristics of tumbled porcine muscle tissue. J Food Sci 43: 1514.

Chen, CM, Trout, GR. 1991. Color and stability in restructure beef steaks during frozen
storage: effects of various binders. J Food Sci 56(6):]461-1475.

64

Claus, JR, Hunt, MC, Kastner, CL. 1989. Effects of substituting added water for fat on
the textural, sensory and processing characteristics of bologna. J Muscle Foods 1:1-21.

Claus, JR, Hunt, MC, Kastner, CL, Kropf, DH. 1990. Low-fat, high-added water
bologna: effects of massaging, preblending, and time of addition of water and fat on
physical and sensory characteristics. J Food Sci 55(2):338-345.

Claus, JR, Colby, J W, Flick, GJ. 1994. Processed Meats/Poultry/Seafood. In: Kinsman,
DM, Kotula, AW, Breidenstein, BC, editors. Muscle Foods, Meat, Poultry, Sea Food
Technology. NY: Chapman and Hill. P 106-162.

Craig, J, Bowers, J A, Seib, P. 1991. Sodium tripolyphosphate and sodium ascorbate
as inhibitors of off-ﬂavor development in cooked, vacuum-packaged, ﬁ'ozen turkey. J
Food Sci 56(6): 1529-1531.

Daniel, JR, Weaver. CM. 2000. Carbohydrates: Functional properties. In: Christen, GL,
Smith J S, authors. Food Chemistry: Principles and Applications. West Sacramento, CA:
Science Technology System. P 55-77.

Davis, CE, Townsend, WE, Mercuri, AJ. 1975. Effect of polyphosphates on low quality
(PSE) hams during processing. J Anim Sci 41:1632-1637.

DeFreitas, Z, Sebranek, JG, Olson, DG, Carr, JM. 1997. F reeze/thaw stability of cooked
pork sausage as affected by salt, phosphate, pH, and carrageenan. J Food Sci 62(3):551-
554.

Donohowe-Greener, I, Fennema, O. 1993. The effects of plasticizers on crystallinity,
permeability, and mechanical properties of methylcellulose ﬁlms. J Food Process Preserv
17:247-257.

Dutson, TR. 1983. The measurement of pH in muscle and its importance to meat
quality. Reciprocal Meats Conference Proceedings 36:92.

Dziezak, JD. 1990. Phosphates improve many foods. Food Technol 44(4):80—92.

Ellinger, RH. 1972. Phosphates in food processing. In: Furia, TE, editor. Handbook of
Food Additives, 2nd Ed. Cleveland, OH: CRC Press Inc.

Flores, HA, Kastner, CL, Kropf, DH, Hunt, MC. 1986. Effects of blade tenderization and
trimming of connective tissue on hot-boned, restructured, pre-cooked roasts from cows. J

Food Sci 51:1176-1179.

Foegeding, EA, Ramsey, SR. 1986. Effect of gums on low-fat meat batters. J Food Sci
51:33-35, 46.

65

Foegeding, EA, Ramsey, SR. 1987. Rheological and water holding properties of gelled
meat batters containing iota carrageenan, kappa carrageenan or xanthan gum. J Food Sci
52(3):549-553.

Frank, P. 2000. Adding Value to Meat Products. Food Product Design (December):75-
103.

Gaska, MT, Regenstein, JM. 1982. Timed emulsiﬁcation studies with chicken breast
muscle. Soluble and insoluble myobﬁbrillar proteins. J Food Sci 4721438.

Gillett, RAN, Carpenter, JA. 1992. Effects of binding substrate, type of non-meat
additive and method of tenderizing on cured chicken rolls. J Food Qual 15:225-23 8.

Gillett, TA, Meiburg, DE, Brown, CL, Simon, S. 1977. Parameters affecting meat
protein extraction and interpretation of model system data for meat emulsion formulation.
J Food Sci 42:1606-1610.

Glicksman, M. 1969. Gum Technology in the Food Industry. NY: Academic Press.
Glicksman, M. 1983. Red seaweed extracts (agar, carrageenans, furcellaran). In:
Glicksman, M, editor. Food Hydrocolloids Vol. 11. Boca Raton, FL: CRC Press Inc.

P 73-107.

Grover, JA. 1982. Methylcellulose and hydroxmethocellulose. In: Glicksman, M editor.
Food Hydrocolloids, Vol. HI. Boca Raton, FL: CRC Press Inc. P 122-153.

Grover, JA. 1986. Food Hydrocolloids, Vol IH. Glicksman, M, editor. Boca Raton, FL:
CRC Press Inc. P 121-154.

Hall, CW, Farrall, AW, Rippen A1. 1986. Encyclopedia of Food Engineering, 21nd Ed.
CT: AVI Publishing Company Inc. P 882.

Halliday, DA. 1978. Phosphates in food processing. Processing Biochem 13(7):6.
Hamm, R. 1960. Biochemistry of meat hydration. Adv Food Res 10:355-463.

Hamm, R. 1972. Koilloidchemie des Fleisches. Parey, P, editor. Berlin, Hamburg.
P 274.

Hamm, R. 1981. Post-mortem changes in muscle as affecting the quality of comminuted
meat products. In: Lawrie, RA, editor. Developments in Meat Science, Vol. 2. London:
Pergamon Press.

66

Hamm, R. 1985. The effect of water on the quality of meat and meat products: Problems
and research needs. In: Simatos, D, Multon IL, editors. Properties of Water in Foods.
NATO ASI Series B: Applied Science No. 90. Martinus Nijhoff Publications. Dordrecht,
Netherlands. P 591-602.

Hamm, R. 1994. The influence of pH on the protein net charge in the myoﬁbrillar
system. Reciprocal Meat Conference Proceedings 47:5-9.

Hand, LW, Hollinsgworth, CW, Calkins, CR, Mandigo, RW. 1987. Effects of pre-
blending, reduced fat and salt levels on frankfurter characteristics. J Food Sci 52:1149-
1 151.

Hawley, RL, Tuley, WB. 1976. Method of protein fortiﬁcation of extra pumped meats.
US. Patent 3,989,851.

Hedrick, HB. Aberle, ED, Forrest, JC, Judge, MD, Merkel, RA. 1989. Principles of Meat
Science, 3rd Ed. IA: Kendal/Hunt Publishing Co. P 1-344.

Hegenbart, S. 1996. Understanding Starch Functionality. Food Product Design
(January):23-34.

Hill, SE, Prusa, KJ. 1988. Physical and sensory properties of lean ground beef patties
containing methylcellulose and hydroxypropyl methylcellulose. J Food Qua] 11:331-337.

Hirren, M, Desbrieres, J, Rinaudo, M. 1996. Physical properties of methylcellulose in
relation with the conditions for cellulose modiﬁcation. Carb Poly 31:243-252.

Holownia, KI, Erickson, MC, Chinnan, MS, Eitenmiller, RR. 2001. Tocopherol losses in
peanut oil during pressure frying of marinated chicken strips coated with edible ﬁlm.
Food Res Int 34:77-80.

Honikel, KO. 1987. Critical evaluation of methods detecting water-holding capacity in
meat. In: Romita, A, Valin, C, Talyor, A, editors. Accelerated Processing of Meat.
London: Elsevier Applied Science. P 225-239.

Honkavaara, M. 1988. Inﬂuence of PSE pork on the quality and economics of cooked,
cured ham and fermented dry sausage manufacture. Meat Sci 24:201-207.

Honkavaara, M. 1990. Effect of PSE pork on the processing properties of cooked meat
products. F leishwirtsch Int. 2:20-22.

Howling, D. 1980. The inﬂuence of the structure of starch ion and its rheological
properties. Food Chem 6:51.

67

Huffman, DL, Cordray, J C. 1982. Processing systems-particle reduction systems
(grinding, ﬂaking, chunking, slicing). Proc. of Meat Science and Technology,
International Symposium. National Live Stock and Meat Board, Chicago, IL. P 229.

Ingram, M, Kitchell, AG. 1967. Salt as a preservative for foods. Food Technol 2:1.

Jeremiah, LE. 1986. Effects on inherent muscle quality differences upon the palatability
and cooking properties of various fresh, cured and processed pork products. J Food Qual
9:279-287.

Jonas, JJ, Craig, TW, Huston, RL, Marth, EH, Speckrnan, EW, Steiner, TF, Weisberg,
SM. 1976. Dariy products as food protein resources. J Milk Food Technol 39:778.

J ones, SL, Carr, TR, McKeith, FK. 1987. Palatability and storage characteristics of
precooked pork roasts. J Food Sci 52:279.

Kauffman, RG, Marsh, BB. 1987. Quality characteristics of muscle as food. In: Price, JF,
Schweigert BS, editors. The Science of Meat and Meat Products, 3rd Ed. Westport, CT:
Food & Nutrition Press, Inc. P 349-3 70.

Kardouche, MB, Pratt, DE, Stadelman, WJ. 1978. Effect of soy protein isolate on
turkey rolls made from pre- and post-rigor muscle. J Food Sci 43:882.

Keeton, JT, 1983. Effect of fat and NaCl/phosphate levels on the chemical and sensory
properties of pork patties. J Food Sci 48:878-881.

Keeton, JT. 2001. Formed and emulsion products. In: Sams, AR, editor. Poultry Meat
Processing. Boca Raton, FL: CRC Press Inc. P 196-225.

Kinsella, JE. 1976. Functional properties of soy proteins. J Am Oil Chem Soc. 56:242-
258.

Konstance, RP, Strange, ED. 1991. Solubility and viscous properties of casein and
caseinates. J Food Sci 56(2):556-559.

Krause, RJ, Ockerman, HW, Krol, B, Moerrnan, PC, Plimpton, RF. 1978. Inﬂuence of
tumbling, tumbling time and sodium tri polyphosphate on quality and yield of cured
hams. J Food Sci 43:853.

Lewis, DF, Groves, KHM, Holgate, JH. 1986. Action of polyphosphates in meat
products. Food Microstr 5:53.

Lin, GC, Mittal, GS, Barbut, S. 1990. Effects of tumbling speed and cumulative
revolutions on restructured hams' quality. J Food Process Preserv 14:467-479.

68

Lindsay, RC. 1985. Food additives. In: Fennema, OR, editor. Food Chemistry, 2“d Ed.
New York, NY: Marcel Dekker, Inc. P 629-688.

Mandigo, RW. 1976. Flaked and formed meats. In: Carpenter, JA, editor. Proceedings
18th Annual Meat Science Institute. Athens, GA: University of Georgia, Food Science
Dept. P 29-34.

Maurer, AJ. 1979. Extrusion and texturizing in themanufacture of poultry products.
Food Technol 33(4):48.

McCormick, D. 1982. Reconsidering applications for the formed and restructured protein
foods. Prepared Foods. Nov. 1982. P 101-104.

Megard, D, Kitabatake, N, Cheftel, J C. 1985. Continuous restructuring of mechanically
deboned chicken meat by HTST extrusion cooking. J Food Sci 50:1364-1369.

Meilgaard. M, Civille, GV, Carr, ET. 1991. Sensory Evaluation Techniques, Boca Raton,
FL: CRC Press Inc.

Miller, M. 1989. Will PSE be Pork's Next Challenge? Pork 1989. 9(1):66-69.

Miller, R. 2000. Functionality of non-meat ingredients used in enhanced pork. In:
National Pork Board Pork Quality Facts. 1998. Des Moines, LA. P 1-10.

Mittal, GS, Barbut, S. 1993. Effects of various cellulose gums on the quality parameters
of low-fat breakfast sausages. Meat Sci 35:93-103.

Motzer, EA, Carpenter, JA, Reynolds, AE, Lyon, CE. 1998. Quality of restructured hams
manufactured with PSE pork as affected by water binders. J Food Sci 63: 1007-101 1.

Mustakas, GC, Sohns, VB. 1976. Soy processes, equipment, capital and processing
costs. USDA FCS Research Report 33:18.

Nold, RA, Romans, JR, Costello, WJ, Libal, GW. 1999. Characterization of muscles
from boars, barrows and gilts slaughtered at 100 or 110 kilograms: differences in fat,
moisture, color, water-holding capacity and collgen. J Anim Sci 77: 1746-1757.

Northucutt, JK, F oegeding, EA, Edens, FW. 1994. Water-holding properties of thermally
preconditioned chicken breast and leg meat. Poult Sci 73:308-316.

Ockerman, HW, Organisciak, CS. 1978. Diffusion of curing brine in tumbled and non-
tumbled porcine tissue. J Food Protec 41:178.

Offer, G, Knight, P. 1988. The structural basis of water holding in meat. Part 1: general

principles of water uptake in meat processing. In: Lawrie, R, editor. Developments in
Meat Science, Vol. 4. London, NY: Elsevier Applied Science. P 64-190.

69

Offer, GW, Trinick, J. 1983. On the mechanism of water holding in meats; the swelling
and shrinking of myoﬁbrils. Meat Sci 82245-281.

Osbum, WN. 1996. Improving the Functionality of Recovered Connective Tissue
Proteins. [DPhil dissertaion]. Lincoln, NE: University of Nebraska. 255 p. Available
from: Lincoln, NE.

Osbum, WN. 2001. Graduate course: FSC 433-Food Processing: Muscle Foods.
Michigan State University, East Lansing, MI.

Pearson, AM, Tauber, F W, [editors]. 1984. Processed Meats, Second Edition. Westport,
CT: AVI Publishing Co., Inc.

Pearson, AM, Gillett, TA. 1996. Introduction to meat processing, Raw materials;
sectioned and formed meat products; sausages; casings, extenders, and additives.
Processed Meats, 3rd Ed. New York, NY: Chapman and Hall. P 1-22, 126-143, 144-179,
210-241, 291-310.

Porcella, MI, Sénchez, G, Vaudagna, ML., Zanelli, AM, Meichtri, LH, Gallinger, MM,
Lasta, J A. 2001. Soy protein isolate to vacuum-packaged chorizos: effect on drip loss,
quality characteristics and stability during refrigeration storage. Meat Sci 57:437-443.

Prabhu, GA, Sebranek, JG. 1997. Quality characteristics of ham formulated with
modiﬁed cornstarch and kappa-carrageenan. J Food Sci 62(1): 198-202.

Rees, DA. 1969. Structure, conformation. and mechanism in the formation of
polysaccharide gels and networks. Adv Carb Chem Biochem 24:267.

Rees, DA. 1972. Polysaccharide gels. A molecular view. Chem Indus 16:630.

Rhee, KS. 1978. Minimization of further lipid peroxidation in the destillation 2-
thiobarbutiric acid test of ﬁsh and meat. J Food Sci 43:1776-1778.

Rinaudo, M. 1988. Gelation of ionic polysaccharides, in gums and stabilizers for the
food industry. Phillips, GO, Williams, PA, Wedlock, DJ, editors. Oxford: IRL Press.

P 119.

Romans, JR, Costello, WJ, Carlson, CW, Greaser, ML, Jones, KW. I994. Beef
identiﬁcation and fabrication, Fresh meat processing, Meat curing and smoking,
Sausages, Structure and function of muscle. In: The Meat We Eat. Danville, IL: Interstate
Publishers, Inc. P 543-596, 643-686, 727-772, 773-886, 887-904.

Rust, R, Olson, D. 1988. Making Good "Lite" Sausage. Meat and Poultry 34(6): 10.

SAS Institute, Inc. 2002. SAS User’s Guide, Version 8.2. Cary, NC: SAS Institute.

70

Schmidt, G, Trout, G. pH and Color. 1984. Meat Ind. 30(8):30,33.

Schwartz, WC, Mandigo, RW. 1976. Effect of salt, sodium tripolyphosphate, and storage
on restructured pork. J Food Sci 41: 1266-1269.

Schweiger, RG. 1974. Soy protein concentrates and isolates in comminuted meat
systems. J Am Oil Soc 51:192A.

Sebranek, JG, Olson, DG, Whitting, RC, Benedict, RC, Rust, RE, Kraft, AA, Woychik,
JH. 1983. Physiological role of dietary sodium in human health and implications of
sodium reduction in muscle foods. Food Technol 37(7):51.

Secrist, JL. 1982. Long-Term Reasearch Needs and Goals. Proceedings: Int Symp Meat
Sci and Technol. National Live Stock & Meat Board, Chicago, IL. P 289.

Shand, PJ, Sofos, JN, Schmidt, GR. 1993. Properties of algin/calcium and salt/phosphate
structured beef rolls with added gums. J Food Sci 58(6):1224-1230.

Shand, PJ, Sofos, JN, Schmidt, GR. 1994. Kappa-carrageenan, soditun chloride and
temperature affect yield and texture of structured beef rolls. J Food Sci 59(2):282-287.

Shand, PJ, Boles, JA, Patience, JF, McCurdy, AR, and Shaefer, AL. 1995. Acid/Base
Status of Stress Susceptible Pigs Affects Cured Ham Quality. J Food Sci 60(2):996-1000.

Shimp, LA. 1981. The advantages of STPP for cured meat production. Meat Processing
(August) 65.

Siegel, DG, Schmidt, GR. 1979. Ionic, pH and temperature effects on the binding ability
of myosin. J Food Sci 44:1686-1689.

Siegel, DG, Tuley, WB, Norton, HW, Schmidt, GR. 1979. Sensory, textural, and yield
properties of. combination ham extended with isolated soy protein. J Food Sci 44: 1049-
105 1.

Skrede, G. 1989. Comparison of various types of starch when used in meat sausages.
Meat Sci 25:21-36.

Smith, DM, Culbertson, JD. 2000. Protiens: Functional Properties. In: Christen, GL,
Smith, J S. Food Chemistry: Principals and Applications. USA. Science Technology
System. P 131-148.

Smith, DM. 2001. Functional properties of muscle proteins in processed poultry products.

In: Sams, AR, editor. Poultry Meat Processing. Boca Raton, FL: CRC Press Inc. P 181-
194.

71

Smith, LA, Simmons, SL, McKeith, FK. Bechtel. PJ, Brady, PL. 1984. Effects of sodium
tripolyphosphate on physical and sensory properties of beef and pork roasts. J Food Sci
49:1636-1637.

Sofos, JN. 1986. Use of phosphates in low-sodium meat products. Food Technol
(September):52-69.

Solomon, LW, Schmidt, GR. 1980. Effect of vacuum and mixing on the extractability
and functionality of pre- and post-rigor beef. J Food Sci 45:283.

Southward, CR. 1985. Manufacture and applications of edible casein products. In:
Manufacture and properties. New Zeal J Dairy Sci Technol 20:79

Soy Protein Council. 1987. Soy protein products; characteristics, nutritional aspects, and
utilization. Washington DC: Soy Protein Council. P 1-43.

Steinhauer, JE. 1983. Food phosphates for use in the meat, poultry and seafood industry.
Dairy Food Sani 3(7):244.

Steinke, LW. 2001. Moisture management and texture enhancement of chicken patties
containing methylcellulose [MS thesis] East Lansing, MI: Michigan State University. 123
p. Available from: Michigan State University.

Su, YK, Bowers, JA, Zayas, J F. 2000. Physical characteristics and microstructure of
reduced-fat ﬁ'ankfurters as affected by salt and emulsiﬁed fats stabilized with non-meat
proteins. J Food Sci 65(1):]23-128.

Tarladigis, GG, Wats, BM, Younthan, MT, Dugan, L Jr. 1960. J Am Oil Chem 37:44-48.

Trius, A, Sebranek, JG, Rust, RE, Carr, JM. 1994a. Low-fat bologna and beaker sausage:
effects of carrageenans and chloride salts. J Food Sci 59(5):941-945.

Trius, A, Sebranek, JG, Rust, RE, Carr, JM. 1994b. Carrageenans in beaker sausage as
affected by pH and sodium tripolyphosphate. J Food Sci 59(5):946-951.

Trius, A, Sebranek, JG. 1996. Carrageenans and their use in meat products. Crit Rev
Food Sci Nutr 36(1-2):69-85.

Trout, GR, Schmidt, GR. 1983. Utilization of phosphates in meat products. Reciprocal
Meat Conference Proceedings 36:24-27.

Troutt, ES, Hunt, MC, Johnson, DE, Claus, JR, Kastner, CL, Kropf, DH. 1992.
Characteristics of low-fat ground beef containing texture-modifying ingredients. J Food
Sci 57(1):]9-24.

Trudso, JE. 1985. Increasing yields with carrageenan. Meat Processing 24(2):37-42.

72

Uram, GA, Carpenter, JA, Reagan, JO. 1984. Effects of emulsions, particle size and
levels of added water on the acceptability of smoked sausage. J Food Sci 49:966-967.

USDA. 2001. Code of Federal Regulations, Title 9 and Title 21. Web page.
USDA. 2002. Food and Drug Administration. http://www.fda.gov/.
USDA. 2002. Food Safety and Inspection Service. http://vwwv.fsis.usda.gov/.

Van den Hoven, M. 1987. Functionality of dairy ingredients in meat products. Food
Technol 41(10):72.

Vote, DJ, Platter, WJ, Tatum, JD, Schmidt, GR, Belk, KE, Smith, GC, Speer, NC. 2000.
Injection of beef strip loins with solutions containing sodium tripolyphosphate, sodium
lactate, and sodium chloride to enhance palatability. J Anim Sci 78:952-95 7.

Whiting, RC. 1984. Addition of phosphates, proteins, and gums to reduced-salt
frankfurter batters. J Food Sci 49:1355-1357.

Whiting, RC. 1987. Inﬂuence of various salts and water-soluble compounds on water and
fat exudation and gel strength of meat batters. J Food Sci 52(5):] 130-1132, 1158.

Whiting, RC. 1988. Ingredients and processing factors that control muscle protein
functionality. Food Technol 42(4): 104-1 14, 210.

Whiting, RC. 1989. Contributions of Collagen to the Properties of Comminuted and
Restructured Meat Products. Reciprocal Meat Conference Proceedings. 42: 149-154.

Wismer-Pedersen, J. 1960a. Effect of cure on pork with watery structure. 1. Binding of
salt and water to the meat. Food Res 25:789-798.

Wismer-Pedersen, J. 1960b. Effect of cure on pork with watery structure. I]. Effect on
quality of canned hams. Food Res 25:799-801.

Wood, JD. 1985. Consequences of changes in carcass composition of meat quality. In:
Haresign, W, Cole DJA, editors. Recent Advances in Animal Nutrition, 1St Ed.
Butterworths, London. P 157-166.

Wotton, M, Chaudhry, MA. 1979. Eneymic digestibility of modiﬁed starches. Starch
31(7):224-228.

Ziegler, GR, Acton, J C. 1984. Mechanisms of gel formation by protein of muscle
tissue. Food Technol 38:77.

Zipser, MW, Watts, BM. 1962. Lipid oxidation (TBA) methods. Food Technol
16(7): 102.

73

CHAPTER 3
EVALUATION OF HY DROCOLLOID SOLUTIONS TO IMPROVE

FUNCTIONAL ATTRIBUTES OF HIGH MOISTURE RESTRUCTURED HAMS
IN A MODEL SYSTEM

ABSTRACT

Hydrocolloid solutions containing either 0.2, 0.4, 0.6, or, 0.8% methylcellulose (MC),
hydroxypropyl methylcellulose (HPMC) and kappa carrageenan (KC) were evaluated as
purge controllers to determine their effects on high-moisture restructured ham attributes
in a model system. Brine solutions (45% addition w/w) were added to restructured “test
tube” hams, which were subsequently cooked to 70°C internally. Treatment brines
decreased (P<0.05) purge loss by 6.0% and brines containing KC and HPMC had higher
(P<0.05) cook yields. Results suggest that brines formulated with KC and HPMC or MC

will increase cook yields and decrease purge loss.

*Chapter 3 is formatted in manuscript style according to the Journal of Food Science*

Keywords: purge controllers, hydrocolloids, restructured ham

74

Introduction

Hydrocolloids are plant-derived, long-chain carbohydrate polymers. Many
hydrocolloids have the ability to thicken and gel as a solution as well as exhibit meat
gelling, emulsifying and stabilizing properties (Pearson and Gillett 1996). They function
as water-binders in numerous food systems (Glicksman 1969) including restructured
meat products. Approved purge controllers (U SDA-FSIS 2002) allow processors to
manufacture high-added-water products (i.e., hams) while decreasing the negative
impacts of losing this added water during storage (purge).

Hydrocolloid gums such as carrageenan, xanthan gum, and alginates have been
studied in meat and poultry products. However, limited research is available that
investigates the incorporation of methylcellulose (MC) and/or hydroxypropyl
methylcellulose (HPMC) into meat products. MC and HPMC are capable of forming a
gel to bind water during thermal processing. Steinke (2001) showed that chicken patties
manufactured with viscous, supergelling MC at 0.25% had higher cook yields than
control patties (75.5% versus 74.5%, P<0.05). Earlier studies utilizing 1% MC and
HPMC in lean beef patties decreased cook yields (Hill and Prusa 1988). This was further
conﬁrmed with a study utilizing MC (0.2%) in low-fat frankfurters conducted by
Foegeding and Ramsey (1986). Lower viscosity carboxymethyl cellulose and higher
viscosity microcrystalline cellulose were used individually (1% solution) in low-fat
breakfast sausage and were shown to decrease moisture retention after cooking (Mittal
and Barbut 1993). Hill and Prusa (1988) stated that total drip loss after cooking and
evaporative losses for lean ground beef patties increased as the percent MC increased (0.5

to 1.0%), but decreased for HPMC (0.5 to 1.0%). These studies pose a question as to

75

whether the use of MC or HPMC in meat products may decrease purge values as a result
of less available free water in the product after thermal processing (lower cook yields).
The differences in MC and HPMC gel forming ability and viscosity may be the reasons
for differences noted in the meat product attributes investigated in these studies.

The incorporation of different METHOCELTM (The Dow Chemical Co., Midland,
MI) type hydrocolloid gums, such as A4M (MC), F4M and K4M (HPMC) may prove to
enhance the cook yield of higher (45%) added-water products while minimizing purge
during storage due to their gel forming capabilities at various temperatures. An
additional reason for investigating these hydrocolloids is their ability to bind water at
lower usage levels (< 1.0%). Steinke (2001) utilized 0.25% MC (supergelling) in ground
chicken patties and reported increased cook yields. Yet, Hill and Prusa (1988)
demonstrated lower moisture retention with 1.0% MC and HPMC added to beef patties.

Other researchers have utilized different METHOCELTM types singularly in meat
products with differing results. However, the combination of hydrocolloids (MC,
HPMC, KC) has not been studied by others. The combining of MC and/or HPMC with
KC may provide a potential synergistic or additive effect when incorporated into meat
products as a brine solution, thereby promoting water binding and retention during
thermal processing and subsequent storage. Utilizing hydrocolloid gums that gel upon
thermal processing (MC and HPMC) with KC that gels upon cooling following thermal
processing may entrap added water in the cooking and cooling process. Our hypothesis
was that hydrocolloid gums (MC, HPMC, and KC) in a brine solution may participate in
protein-hydrocolloid interactions resulting in a higher water binding and water retention

in high-moisture restructured ham mode] meat system.

76

The ﬁrst objective of this study was to investigate the effects of MC, HPMC, and
KC on water binding, water retention and functional attributes in hydrocolloid water and
brine solutions and in a restructured ham model system. The second objective was to
determine if combinations of hydrocolloids in a brine solution incorporated into a
restructured ham model system demonstrated a synergistic effect on cook yields, purge

values and textural attributes.

77

Materials and Methods

Evaluation of metlr ylcellulose and hydroxypropyl methylcellulose

in water and brine solutions.

Study 1 was conducted in four experiments. Experiment I investigated the
functional properties of selected hydrocolloids in a water solution. Experiment I]
investigated the ﬁmctionality of the hydrocolloids in a brine solution (water, salt,
phosphate as the primary ingredients). Experiment III incorporated various types and
levels of hydrocolloids in brine solutions in a meat model system to determine their
impact on textural and quality attributes. The results from Experiment III determined
which hydrocolloid brine solutions were feasible for commercial restructured ham
manufacture. Experiment IV incorporated a combination of hydrocolloids in a brine
solution within a meat model system to determine if any synergistic effects were

observed with respect to increased water binding and retention during storage.

Experimental Design and Data Analysis

Experiment I and II were designed as a 4 x 4 factorial treatment arrangement with
the main effects of hydrocolloid type (A4M=MC I; F4M=HPMC I; K4M=HPMC II;
KC) and level of incorporation (0.2, 0.4, 0.6, 0.8%) in either a water or brine solution.
Experiment III was designed as a 4 x 4 factorial arrangement of treatments with the main
effects of hydrocolloid type (MC 1, HPMC I, HPMC H, KC) and level of incorporation

(0.2, 0.4, 0.6, 0.8%) in a brine solution. The brines were incorporated into a restructured

78

ham model system and treatments were compared to a control (no hydrocolloid).
Experiment IV was designed as a one-way analysis of variance with four hydrocolloid
brine treatment combinations and a control (no hydrocolloids). All hydrocolloid brine
solutions were added to the ham at 45% (wt/wt). Each experiment was replicated three
times. The level of signiﬁcance for all statistical analyses was determined at P<0.05

(SAS User’s Guide, Version 8.2. Cary, NC: SAS Institute).

Hydrocolloid Ingredients

Methylcellulose (MC) and hydroxypropyl methylcellulose (HPMC) food gums
under the commercial name METHOCELTM (Dow Chemical Company, Midland, MI)
were used. Methylcellulose I (MC 1) is of medium viscosity (4,000 cPs), hydrates below
13°C and forms a ﬁrm gel at 50-55°C. Hydroxypropyl methylcellulose I (HPMC I) is of
medium viscosity (4,000 cPs), hydrates below 25°C, and forms a semi-ﬁrm gel at 62-
68°C. Finally, HPMC H is of medium viscosity (4,000 cPs), hydrates below 295°C, and
forms soft gels at 70-90°C.

The selected KC for these research studies was Gelcarin® ME 6910 (FMC
BioPolymer, Princeton, NJ). Experiments H, IH and IV brine solutions contained salt
(1.8%), sodium tripolyphosphate (STP) (0.3%, Briﬁsol 512, BK Giulini Corporation,
Simi Valley, CA), food grade sugar (0.26%), sodium nitrite (150 ppm) (J .T. Bakeer,
Phillipsburg, NJ.) and sodium erythorbate (250 ppm) (Butcher and Packer Supply Co.,

Detroit, MI).

79

Manufacturing Process
A. Hydrocolloid Water and Brine Solution Manufacturing (Exp. I-IV)

Hydrocolloid water (Exp. 1) and hydrocolloid brine (Exp. 11) solutions (909 g)
were formulated. The hydrocolloid ingredients were used to formulate water or brine
solutions at 0.2, 0.4, 0.6 or 0.8% of the total solution. The solutions were mixed using a
4-blade mixing head attached to a drill (SKIL, S-B Power Tool Co., Chicago, IL). The
hydrocolloid brine solutions also contained salt, STP, sodium nitrite, and sodium
erythorbate at the percentages previously described.

Experiment IV brine solution treatments were: Treatment (TRT) 1: MC I/HPMC
I at 0.4/0.6%, TRT 2: MC I/KC at 0.4/0.6%; TRT 3: HPMC I/KC at 0.6/0.6% and TRT 4:
MC I/I-IPMC I/KC at 0.4/0.6/0.6%, and the control (CONT) brine: no hydrocolloid. All
solutions were covered and stored overnight (12-16 hrs) in a walk-in cooler (2-4°C).

Due to the differences in thermal gelling between MC/HPMC and KC gel plugs
were analyzed for water retention and color at different temperatures. Treatments
containing MC and HPMC are “hot” gelling hydrocolloids; therefore, they were analyzed

at 70°C. Kappa carrageenan forms a gel upon cooling following thermal processing;

therefore, KC was analyzed at 37.8°C.
B. Model Meat System Processing (Exp. [11 and I l0
Fresh pork semimembranosus (IMPS 402F) muscles were obtained from a local
meat company and placed into a cooler 2-4°C. Muscles were denuded and the gracilis
muscle was removed. Muscles were weighed (7.7 kg) according to the appropriate

product formulation for each replication (n=3) and covered with SaranTM wrap.

80

Pork semimembranosus muscle was ground through a 0.9 cm plate twice utilizing
a Toledo chopper (Model- 5126, Toledo Scale Corp., Toledo, OH). Four hundred grams
of freshly ground muscle and 180 g of the designated treatment brine solution were added
to a Hobart Kitchen Aid mixer (Model KS-A, Hobart Corporation, Troy, OH) and mixed
for 3 min at speed setting 2.

C. Thermal Processing

Thirty-four grams (in triplicate) of the designated hydrocolloid water (Exp. 1) or brine
(Exp. H) solutions were placed into 50 mL polycarbonate centrifuge tubes, capped and
then placed into a programmed water bath (Model 9510, PolyScience, Niles, IL) that
mimicked a restructured ham thermal processing schedule. The samples were thermally
processed to an internal temperature of 70°C. The same procedures were followed for
the manufacture of a high-moisture restructured ham in a model system (Exp. HI and IV).
For analyses purposes, thermally processed (70°C) restructured ham was removed from

polycarbonate tubes, resulting in a cylindrical, tube shaped ham sample (i.e. “p1ug”).

Analyses

A. pH determination

Hydrocolloid water and brine solution pH values for all experiments were
determined at 5°C using an Accumet pH Meter (AB 15, Fisher Scientiﬁc, Co., Pittsburgh,
PA). Restructured ham raw and cooked pH values (Exp. III and IV) were determined by
homogenizing one gram of sample with 10 mL of distilled, deionized water using a

Polytron mixer (PT-35, Kinematica, AG, Switzerland).

81

B. Viscosity Analysis in Hydrocolloid Water and Brine Solutions
The viscosity readings of each hydrocolloid water and brine solution (909 g) were
measured in 946.4 mL glass jars (Fisher Scientiﬁc Co., Pittsburgh, PA) using a
Brookﬁeld Viscometer (Model DV-H, Brookﬁeld Engineering, Co., Stoughton, MA) at
speed setting 12. The selected spindle was lowered into the geometric center of the
water or brine solution until the indented ring on the spindle was level with solution
surface. Viscosity readings were recorded in centipoise (cPs) once the displayed
reading was stabilized.
C. Color Analysis
A ColorTec PCMTM Color Meter (Model 6482, ColorTec Associates, Clinton, NJ)
with a 10° standard observer and an 8 mm reading oriﬁce was used to measure the
exterior surface color of thermally processed (70°C) hydrocolloid water and brine gels
(Exp. I and II). The ColorTec was programmed to analyze L* (lightness), a* values
(Commission Internationale De L’Eclairage (CIE)), with a D65 illuminant (daylight
illuminator), and calibrated on standard white and black tiles. For Experiments HI and IV
the same procedures were utilized to determine the color (L* (lightness), a* (redness),
and b* (yellowness)) values of the interior surface of thermally processed (70°C)
restructured ham plugs. Three readings per gel or ham sample were taken and averaged.
D. Water Retention (Exp. 1 and II)
Hydrocolloid water and brine solutions (34g) containing MC or HPMC were
placed in 50 mL polycarbonate centrifuge tubes and thermally processed (70°C internal
temperature) in a programmable water bath. Solutions containing KC were removed

after cooling to an internal temperature of 378°C, and the tubes were inverted and

82

allowed to drip for 1 min. Sample exudate was collected, weighed and water retention
values were determined as a percentage of initial weight.
E. Cooked Product Yield and 7-day Purge (Exp. 11] and 1 V)

Cooked product yield determinations for restructured hams manufactured in a model
system were performed after the ham plugs were thermally processed (70°C) and cooled
to an internal temperature of 37.8°C. The tubes were inverted and the water released
from the ham samples was collected. Weights (raw meat, cooked meat, polycarbonate
tube) were recorded and percent cook yield was determined as a percentage of initial
weight. The polycarbonate centrifuge tube containing the remaining ham sample was
recapped and chilled (2-4°C) for 12-16 hrs.

To determine percent purge, chilled restructured ham plugs were removed ﬁom
polycarbonate centrifuge tubes and the sample weight recorded. Ham plugs were
vacuum packaged in 12.7 cm x 22.9 cm bags (Cryovac Sealed Air Corp., Duncan, SC)
and stored in a 2-4°C cooler for 7 days. On day 7, each sample package was reweighed,
the ham sample plugs removed, the ham sample and vacuum bag blotted dry and both
were reweighed. The percent purge loss was determined as a percentage of initial weight.

F. T extural Analysis

Gel Strength/Hardness (Exp. 1 and II)

The gel strength/hardness of thermally processed hydrocolloid water and brine
solutions was analyzed on a TA-HDi texture analyzer (Texture Technologies
Corporation, Scarsdale, NY) utilizing a 5 kg load cell and a 1.3 cm diameter acrylic probe
attachment (TA-10) 3.5 cm in height. Each hydrocolloid water and brine solution gel

plug was analyzed in the 50 mL centrifuge tubes in which they were thermally processed.

83

Sample tubes were placed in a molded steel pipe ﬁtting placed on a heavy duty platform
(TA-90) to eliminate tube movement and variability during the analysis. The probe
penetrated the gel plug in the geometric center of the sample, depressing the gel 8 mm
before retracting. Peak force was recorded in grams with a cross-head speed of 1.7 mm/s.
G. Texture Proﬁle Analysis (T PA ) :2-cycle Compression (Exp. 11] and [JO

Experiment HI and IV restructured ham samples were analyzed using the 2-cycle
compression test method, utilizing a TA-HDi Textural Analyzer (Texture Technologies
Corporation, Scarsdale, NY). Two circular samples measuring 2.5 cm (dia) x 2.5 cm
(height) were cut from the center of each ham plug. Each sample was weighed and
analyzed. A 5 kg load cell was used to measure hardness, springiness, cohesiveness,
chewiness, and resilience using a 75 mm diameter aluminum cylinder plate (TA-30), on a
heavy duty platform (TA-90). Samples were compressed to 25% of their original height
(75% compression) in a 2-cycle compression at 4-6°C with a crosshead speed of 1.7

mm/s.

84

Results and Discussion

Experiment 1

Signiﬁcant two-way interactions (P<0.01) were observed for hydrocolloid water
solution pH, viscosity, color (L*), water retention, and gel hardness (Figure 2). Kappa
carrageenan pH values were higher than MC I (A4M), HPMC I (F4M), and HPMC H
(K4M) at all levels. The elevated pH value of KC could be attributed to the sulfated units
that KC possesses and allows for KC to be slightly basic (Trius and Sebranek 1996,
Daniel and Weaver 2000) (Figure 2). Viscosity values for all hydrocolloid gums were
similar at 0.2% (Figure 2). As the hydrocolloid percentage increased, the solutions
containing MC 1, HPMC I, and HPMC II were more viscous. A slight increase in
viscosity occurred between 0.2 and 0.4% was observed, but from 0.4 to 0.8%
hydrocolloid addition viscosity values increased to a greater extent. Kappa carrageenan’s
lower viscosity values remained constant at all the levels of addition. The less viscous
solutions demonstrated by KC can be advantageous to the meat processor utilizing a
brine injection systems. Water retention of MC I at all levels (0.2-0.8%) was higher than
all remaining treatments (Figure 2). From 0.2 to 0.4% (MC 1) there was an increase of
approximately 40% water retention and then plateaued from 0.4 to 0.8%. Water retention
for solutions containing KC and HPMC 11 remained consistently lower at all levels.
Treatment HPMC I showed similar results to KC and HPMC H ﬁ'om 0.2 to 0.4%.
However, with the increased addition of HPMC I water retention was improved by more
than 20%. As hydrocolloid addition increased, L* values decreased (data not shown).

Gel hardness values of MC I increased with higher hydrocolloid levels (Figure 2). At

85

 

 

 

TSEIIII _osEILal 6.2+ oxﬂ

 

35 ...w>w..

 

 

 

 

 

.ON
.0?

cm

.0»

cow
ow—

!» ssanouvu 139

 

mosazlll.ozax+_oslol 87.6!

 

35 d5.-

 

 

 

 

 

 

 

 

 

 

 

 

 

 

mmocEmI .00 H

8 or.

Q’I x) nounmu uaivm

co_.c2om Loum>> now .u

 

 

 

 

_SEQIIIIGEIITSEIOI 87L

 

3: dz...

 

 

 

 

 

 

 

o

.om

cop
om?

.- cow
. 93
y con

0mm

(SdO) AJJSOOSIA

 

@gaznllozazlaIBSIOI 310';

 

as .m>m._
3 no to No

 

 

 

 

 

 

 

Illlx

 

 

 

 

 

E885 hm 9“.

A. 935 mac—6...:— _ow 23 £32.30.— ..SNB £338?» Jan ..em Ccdvmv 228.235 $3-33. "N “my—DUE

 

86

0.2% addition, MC I had similar hardness values compared to KC, HPMC I, and HPMC
11. However, from 0.4 to 0.8%, MC 1 had the greatest gel hardness values. These results
were expected as MC I forms a ﬁrmer gel upon heating when compared to HPMC I and
HPMC H (Anonymous 2001). For KC, HPMC l, and HPMC II the observed gel
hardness values were low across all levels of addition, with KC at 0.8% being higher.
Experiment H

Hydrocolloid brine solutions exhibited signiﬁcant (P<0.0001) two-way
interactions for viscosity and water retention values (Figure 3). Brine viscosity values
for all hydrocolloid gums were similar at 0.2% (Figure 3). Kappa carrageenan brine
solutions remained the least viscous at all levels (0.2-0.8%). As the hydrocolloid
percentage increased from 0.4-0.6%, the brine solutions containing MC 1, HPMC I, and
HPMC H were more viscous. From 0.6-0.8% viscosity levels of MC 1, HPMC I, and
HPMC H tended to plateau. The high viscosity values observed may be beneﬁcial for
meat coating systems (Grover 1986; Priya and others 1996; Anonymous 2000); however,
they may be detrimental for injection systems. Water retention values improved with the
increase of hydrocolloid level (Figure 3). Treatments KC, HPMC I, and HPMC H water
retention values were similar at 0.2%. Treatment MC I demonstrated the highest water
retention at 0.2%. However, MC I decreased water retention at 0.4% then increased
water retention ﬁ'om 0.6 to 0.8%. The authors have no explanation for this response;
however, these results suggest that a processor should consider utilizing MC I either
above or below 0.4% for optimum water retention. As the percentage of hydrocolloid
increased, brine solutions containing HPMC II tended to retain higher percentages of

water.

87

 

 

ﬂ 1
EOEQII‘I _ 0201+ _ 0.2+. - Owll’lL

 

33 Juan.
wd od v.0 Nd
u » Lll o

 

 

 

l |. ON
lﬁ ov
-I lw ow

, . on
-1 cow
1 omr

 

 

(%) NouNaiaa 831W

 

 

 

 

__ OEQIIIW _ OEQIIIII .Os_+ oxlolg

 

3: dz:

 

 

 

 

 

 

 

 

cozcogom Loam; 509m

A: Qua 233—3. 05.:— Ee=eoeuPE E 25:39.. .533 can bacon? .5.— Ccccdvmv 25:228.: $3-35. "m 2:”:—

er o
M
. com S
O
,. 84 m
I. o8 m
0
. 8c M.
. 89

 

 

£885 ”mm 9“.

88

No signiﬁcant differences (P>0.05) were seen for pH, L* values, and gel hardness
for hydrocolloid addition levels (Table 3). Kappa carrageenan brine gels were darker
(L*—"40.82), while HPMC I gels were the lightest (L*=69.30). MC I exhibited
signiﬁcantly (P<0.05) higher gel hardness values compared to KC, HPMC I, and HPMC
II. The hydrocolloid brine solution treatments containing HPMC I or HPMC H were
similar in gel hardness while KC formed the softest gel.

Experiment IH

Signiﬁcant two-way interactions (P<0.05) were observed for brine pH, brine
viscosity, restructured ham cook yield, 7-day purge (Figure 4), hardness, chewiness, and
resilience (Figure 5). Brine pH values for all treatments were similar at 0.6% with KC
(Figure 4). The pH values ranged from 7.1 to 7.6 and tended to increase as concentration
increased. Viscosity levels for all treatments at 0.2% were similar to the control (Figure
4). Kappa carrageenan low (6.3 cPs) viscosity measurements are similar to those seen in
Experiment I and II. As the hydrocolloid percentage increased from 0.4 to 0.6%, the
brine solutions containing MC 1, HPMC I, and HPMC IIwere more viscous.

Cook yield values for the control and KC were higher at all levels than MC 1.
HPMC I and HPMC 11 (Figure 4). Trius and others (1994b) demonstrated that the
addition of KC at 0.5% signiﬁcantly decreased cook loss values in beaker sausage when
compared the control. Additionally, hams manufactured with 1.5% KC had increased
cook yield values when compared to the control (Prabhu and Sebranek 1997). Treatment
HPMC I] showed a cook yield increase from 0.6 to 0.8%. Treatment MC I had the
highest cook yield value at 0.4% when compared to HPMC I and HPMC 11. These

results seen for MC I at 0.4% contradict cook yield values seen in experiment 11. Ideally,

89

.32va SEE 2: .«o hobo Bag—5m q
.386. £3.55 .
85:56 :5 mm; m was :8 use. wxm a maﬁa map—w E @2338 28:38 055 038: me $263: _oO_
ﬁasco—co cote—o0 a maﬁa»: coca—cm 055 .
20:80.63 8:0» morn: oocﬁooce ABUV Aowmhﬂomh 0Q 3:222:35 co_mm_EEoUv 830 ._
.Uom «a cows—em out: 20:89??— mo In w
.393 =« uo>o wowﬁog cots—em 2:5 3 page 093 22.886»; mo Agwd-m.cv $54 a
.m_o>o_ =« 55 “comes; E3— 98 Ev..— szUOIHm—E H: use _ owe—3:33:68 Enoch—588.3

.23, 2:80:52; 322303508 .o 3e m2 @5328 558830 was. ”25 226083: .
Amodvg “cabbage bus—mogcwﬁ 2m. E58 553, $9.5an3 Bonﬁre wags: 332 3

 

 

 

w.mm 0.3 0%. «.2 od 30.5 as. no.3; ..NN _va 3.26.53 30
mg 3% 9% m.~m 9mm andn .mdo 0.3m uwdv era: 830
86 ans vs. ems .2. ... ms 30:. no: awms min 05.5
3% we a... ...: a... = 02.5 _ 92,—: _ o: 8.
3964 earth. 13:89.1»:

 

A: Sam—V 333.3. 95.5 22.39.??— ue amen—:2— ?» _._—a £28 .29 .8.— maaoE 9.3:.» .231— um «Bah

90

 

 

 

202.": Ion _ 0.2% If _ 0: LT ox II: 6528 1L

 

as $53
0.0 Qo to No 0.0

 

VOONFO

( 7o) 398M

1m
-..o
.N
m

 

 

 

 

 

 

._ 0.2a... Io: _ 02% no: _ us. If ox In: .5528 1L

 

a». ._m>m:
md v.0 v.0 Nd 0.0
r p h p m“

 

l- lillflli- l--- 8

 

 

 

, no
-.8

 

- mm
ﬂoor
mow

( 96) 013“ )IOOO

 

 

 

 

 

 

ode >3-» new 9“.

29> 5.80 ”3. an

 

 

 

@0551]? 65:1? 6.2+ 87:: 6528le

 

1.. .93
no no to mo 3

 

 

 

.. com

o
o
co

(sac) ALISOOSM

 

 

 

coo F

 

_._ osaxlol _ osaxll 62+ 87.: 49:28le

 

3 dz:
2 co to No 0.0

 

.P F p r Q.®

 

I - .l. ,l Illl l - m6
.Illll|lll Ill 1:: +5

 

 

E
. 2 m
2
. I

 

 

 

 

 

ms

 

 

 

 

ms

 

 

£885 2% é. a:

A:— Qnmv 539$ .52: :3:— a 5 555.3. 055 55.8365 .5 5535558 warm—a.»
.5 out:— rma—Yb 6:.“ .55» :25 $5895.» 955 in 25.5 .8.— Amcévmv 2.5.2235 $3.35. 3. ”my—DU:—

Ia octm Nov 9....

91

MC I at 0.4% is creating a protein-hydrocolloid interaction that allows for increased
water binding in a meat system (Figure 4). Overall, lower cook yield values for MC 1,
HPMC I, and HPMC H (except HPMC H 0.8%) were expected as earlier studies utilizing
MC and HPMC at 1.0% in beef patties showed decreases in cook yield values (Hill and
Prusa 1988). Furthermore, a study utilizing 0.2% MC in low-fat frankfurters
demonstrated decreased cook yields when compared to the control (Foegeding and
Ramsey 1986).

From 0.2 to 0.4% hydrocolloid addition, 7-day purge values tended to increase for
all treatments (Figure 4). However, increasing hydrocolloid addition over 0.4%
suggested a decrease in purge values for MC I and HPMC I. Increasing hydrocolloid
percentages from 0.6 to 0.8% tended to increase 7-day purge values for HPMC H and
KC. Overall, MC and HPMC presented lower purge values than KC and the control,
demonstrating METHOCELTM’S ability as a potential purge controller.

Restructured ham hardness values decreased with the increased addition of MC 1,
HPMC I, and HPMC II percentages (Figure 5). In previous studies, Shand and others
(1993) indicated that there is general softening effect with the addition of MC that
decreases binding and textural values. However, KC did suggest that with increased
addition there was improved product hardness. These results conﬁrmed data reported by
DeFreitas and others (1997) that stated the addition of 0.5% KC increased hardness of
pork sausage. Restructured beef rolls with 0.5 and 1.0% KC showed a signiﬁcant
increase in hardness when compared to the control (Shand and others 1994). Chewiness
values for KC increased from 0.2 to 0.4%, then plateaued from 0.4-0.6% and ﬁnally

decreased from 0.8% (Figure 5). Treatments MC 1, HPMC I, and HPMC H steadily

92

 

 

=§+_E+_g+ox+g8+

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

93

 

 

3.396..
ed md v.0 Nd ed
p b r r o

f ill .I. - l ..o u

3

l u 3 m

.h

i 3 m.

-IX-L ...o m

md
on 9“.
TEITQEJIQLonl-LEESIT __oz%+_oz%+_oz+ 9.1-: 6528*
3%... SEE
. . . . . no no 3 mo 2 H
8 mo 3 No 3 l . . _ _ o v
o o u
H . om N
1.. 8m 3 a
m 8. w
1. OS? N I!
1 82m, - 8. u
l w
88 8. m
I an on an 9...

.5893 .55... :3... a 5 2.5.53. 255 55.89.65 .... 596. unit... .53
3.5.3.55“... ......— co..=.o=...mo.. .5 3.358.. ...... £8532? £8525 ...... :25...va 2.5.2285 53535. “n “my—DUE

became less chewy with the increased addition of hydrocolloid percentages. Resilience
values were similar for all treatments at 0.2% (Figure 5). Kappa carrageenan increased
resilience values at higher hydrocolloid addition levels. Resilience values for MC 1,
HPMC I, and HPMC H suggest that at increased percentages product resilience is
decreased. Resilience is deﬁned as the products ability to retain its bound form when
subjected to outside (texture analyzer) forces. These results suggest that the addition of
MC or HPMC will decrease the products ability to withstand environmental factors (i.e.
textural analysis, slicing. packaging. etc.)

Signiﬁcant main effects were seen for meat sample raw pH, cooked pH,
springiness and cohesiveness (Table 4). Raw restructured ham treatment pH values
ranged from 6.09 to 6.15 with the control and KC having the highest pH values. Cooked
restructured ham treatment pH values ranged from 6.25 to 6.33 and level pH values
ranged from 6.25 to 6.33. The control and KC tended to have higher pH values than MC
I, HPMC I, and HPMC II. Control cooked ham had higher pH values than treatments,
with the exception of 0.8% level of addition. These pH values are important as water
binding and retention is partially dependent upon pH. At higher pH levels, the proteins
become more negatively charged, thus repelling each other and allowing for the
myoﬁbrillar proteins to swell and retain water, resulting in increased WHC (Hamm 1994;
Osbum 2001). In general, a pH at 6.0 is the most effective at increasing water and
processed meat binding. At pH 6.0, the gelling and binding of proteins myosin and
actomyosin is ideal (Dutson 1983).

Color values (L*, a*, b*) were not different (P<0.05) (Table 4). The control and

KC were approximately 2 points higher in L* values resulting in a lighter cooked

94

.GodAe 38%? “oz .2

.22va 586 05 mo 8:0 23:85 __
.A_<\~<V commmoEEOo “we 05 wEBw “m5 3 8633800 EN 05 mats—o 3.8 8.8 2563 MO 038 05 3 3053850..
.:o_mmoEEoo 958m 28 SE 05 5933 £382 v08 05 £32— 05 mm ﬂop—ESE?
4582.3 .936 .98: a can 82m ES 2. £3 93— mm m a maﬁa 868.980 293 -N ”mix—«S. 2:05 23:8,:
egos—no.8 85200 a wEnzmS cows—cm 05.5 20:82??— vo=ow MOTH: 8:38:ch ”Am—UV Aowgm—omh on Beets—p.35 :oiﬂSEoUv 830»

.0... a ma 22 3.80.
.0... a ma 5:3 82 as. .

.momb =« $5 8923.. Econ. :38 26 5528 05.5 8 32:. 25 20:88??— mo Aﬁcwdédv .33 u

205— =~W co>o “omega EVM can 3:...— spawnvOIHm—E
= tan _ 822—83598 _.aoaxxohc»: .23.. Eamoomhmdz _ owe—3:02.388 639 E). @58200 cacoowmtmo 393— 6an EEBRESE o
.GodVE “Shoat—u bug—momma? 8m £50.. £55, mar—839m EEob% wags: $802 a-..

 

 

 

md m6 ed ed ad 56 md wd ed 56 5o m2 33:023ch

_.o .g ...: ...; ._ .... ._ .2 .3 ...3 ...: ...: .3 RES masmsam

.oasuuoh

md o.N_ 9.2 _.N_ 0.3 0.2 w.m_ 5.2 m.N_ N.N_ QS ngb

m6 _._ m._ N...— _._ o._ W. m._ N; 5o o._ m2...“

Wm 9N0 5N0 _.mo ”N0 oéo _.mc _.Nc 9N0 mic 04% m2...—

125

:3 gone .30 .30 some .mg .03 .03 .26 acme .03 kg :80

So ...; 2c .2 .c ..._ _.c ..N. .c .m _ .c as... .93 ...; _.o ..2 .o .2.» kg 3.x
32mm 2. a... ...: N... o... a 02.:— _ 92.5 . u: u: .235

.295.— .2—3. 26:89.ch

 

A:— 35 889?. :3:— EEE a 5
28:38 95.5 22.396.2— 5? 62:35:58 8.:— eouaosbme be 9:58. can ...38 in 58 2:3:— ouaacm .23.— 3 03:.

95

ham product when compared to MC I, HPMC 1, and HPMC II. Prabhu and Sebranek
(1997) suggest no color differences were seen with the addition of 1.5% KC in ham when
compared to the control. However, Mittal and Barbut (1993) reported that low-fat
cooked breakfast sausage containing 1% carboxymethyl cellulose decreased D" values
compared to low-fat breakfast sausage containing no hydrocolloid gums. Higher a* and
b* values were observed in treatments containing MC I, HPMC I, and HPMC 11. These
results suggest a trend that MC 1, HPMC 1, and HPMC II may have the potential to
improve added water restructured ham meat color by decreasing the dilution muscle
protein.

Addition of hydrocolloid gums decreased springiness (mm/g) (Table 4). The
control was the springiest treatment with HPMC H being the least springy. These results
may be due to the decrease in protein-protein interactions and an increase in protein-
hydrocolloid interactions, consequently producing a softer, less springy product.
Treatment HPMC I was the most cohesive and treatments MC I and HPMC II were the
least cohesive.

Finally, screening for treatments to be utilized in experiment IV was established
upon consideration of cook yield and purge values with textural hardness. Throughout
experiment HI, HPMC II at 0.2, 0.4, and 0.6% suggested the least amount of water
retention (cook yield, purge) (Figure 4) and the soﬁest texture. In addition, HPMC H at
0.8% exhibited high cook yields (100%). However, it also demonstrated the highest
purge loss (7.8%) as well as soft, crumbly texture thereby eliminating HPMC II from
consideration in experiment IV (Figure 4). Treatments MC 1, HPMC I, and KC were

selected for ﬁirther use. In the evaluation of hydrocolloid addition levels, it was found

96

that MC I at 0.4%, HPMC I at 0.6%, and KC at 0.6% combined the most effective
combination of increased cook yields, decreased purge values with adequate textural
ﬁrmness.
Experiment IV

Signiﬁcant differences (P<0.05) were observed for brine viscosity, cook yield,
color (L*), 7-day purge (Table 5), hardness, cohesiveness, chewiness, and resilience
(Table 6). No signiﬁcant differences (P<0.05) were observed for brine pH, restructured
ham raw pH, cooked pH, color (3* and b* values) (Table 5) and springiness (Table 6).
Treatments (TRT) within this study are deﬁned as TRT 1: MC I/I-IPMC I at 0.4/0.6%,
TRT 2: MC I/KC at 0.4/0.6%; TRT 3: HPMC I/KC at 0.6/0.6% and TRT 4: MC I/HPMC
I/KC at 0.4/0.6/0.6%, and the control (CONT) brine: no hydrocolloid.

Hydrocolloid brine pH values for all treatments ranged ﬁ'om 7.23 to 7.37 (Table
5). Raw meat model pH values ranged from 6.35 to 6.43 and cooked pH values ranged
from 6.50 to 6.56 (Table 5). Hydrocolloid brine solution viscosities ranged from 6.3 to
7783.3 centipoise (cPs). Treatment 1 and 4 brines were the most viscous (>7600 cPs).
The CONT was signiﬁcantly the least viscous (P>0.05) brine at 6.3 cPs. This result was
expected as the CONT was a traditional brine solution with no hydrocolloids added.

Restructured ham L* values for the CONT were higher (P<0.05) than TRT’s 1 to
4. Treatments 1 to 4 had lower D“ values suggesting that the addition of MC or HPMC
will improve added water ham color by decreasing reﬂectance, creating a darker cured
meat color (Table 5). Treatment 1 tended to have higher a* values and the CONT had the

least redness (a*). These results are in support the theory that the addition of water

97

.0000. 580.20... .02 .2
.953 500.2 05 .5 5.5 555m 2
00.95.00 50: 50.5.0502 6053.08 52.0.3 .5 05.... 5020.. 55$ 2.

00.050200 0055.00 0 w55=§ Dov 0.0 003500 50.0.00 .005 .0005 Eu: 00.5.0500. 000.000 05
5 00580 05.05 05 :0 F50 000.0550» A03 000500.. 6...: 3:800:05 ABUV 350555..— 0Q 30.5.0825 55055508 5.00.
00— n .5 050500.50. .0585 :0 8 000.80 5.5 00500503“ .2: 05503 3355503 000500 n25.» 0.000 .
.0... a :0 .82. 08.80 ..
.0... 2. .... .02.. as. _
.000 .0 Ammov 0055500 5 BSA—0:0 500003 055..
.000 2. 2002.0... 0...... 00 :0 .
50.005 .008 050 55.58 055 2 0020.0 0%. 50:08:05 5 5x006 a. to 5.8 .054 ..
. 2... 2.00.0050... “. 08.2.8152:
302022200. .23. 2.000050: u. 08.2.8350... .0 .00 ms. 0.0.8.00 2.500050 00...... 0.5 0.2.08.0»: .
.Amodva: 50.00.50 3:805:50 08 03.: 555.5 85.800053 50.00.55 w5>5 05002 ....

 

 

 

N0 .0. .00 .0. ...... ...; 2005.. an: .x.
.0 0... S. 0... 00.0. m... .2...
N0 0.. 0.. N. 0.. 0.0 .2 .0
0.0 .30 .30 ....00 .000 .000 ....

.550

...0 .000. .000. .000 .000 .000 .20; .80 ...
00.0 00.0 3.0 00.0 00.0 00.0 .2 ...... .80
~00 00.0 9.0 2.0 00.0 0.20 .2 5.. 33.
~00 .20: .3080 0.0.0. .0002 .....0 ......3 0.885 2......

..00 02 02 mm... as 2... .2 ...... 0......

.200 0.0 \ 0.0 . ....0 0.0 \ 0.0 0.0 . 0.0 0.0 . ...0 0.0 ...:3

 

0v:— UEA—E Us UV!— U—Zm: 0!: 02 u 022::— US 5.5—8.0

 

.00.... 0.2.822:

 

.5000»... .005 .0105 a 5 55.58 05.5 50:895.:— 5 055055500 "5.0:; 55..» 505300555
55 assuage...— a .5 out... .0575 can .550 .25» 580 .30— ..37605.» 05.5 .5.— muaoﬁ 0.3.50 .304 "m 050,—.

98

dilutes the concentration of proteins that are responsible for meat color (Miller 2000)
which can result in a paler product color with the use of a CONT brine solution. The b*
values were similar.

Treatments 1 and 2 had lower cook yield values than the control or TRTs 3 and 4.
However, all these cook yield values are greater than 95%, thereby deeming the addition
of hydrocolloid gums in combination successful for increasing cook yields when
compared to hydrocolloids gums utilized singularly (Exp III). This suggests that the
combination of MC and/or HPMC with KC may create a synergistic effect in which cook
yields are increase by more than 10% when compared to experiment III cook yield
values.

The 7-day purge values ranged from 0.8 to 7.4% (Table 5). The CONT exhibited
the highest purge loss of 7.4%, which is consistent with the results from the previous
experiment (Exp III). Treatments 1 to 4 lowered purge loss by at least 6.0% when
compared to the CONT. Treatment 3 displayed the lowest purge loss value of 0.8%.
These results suggest that there are deﬁnite decreases in purge loss while increasing cook
yield values over 95%.

Treatment 3 was signiﬁcantly the hardest (190.0 g) and TRT 1 was the softest
(86.6 g) (Table 6). The addition of MC I and HPMC I (TRTl) together in a brine
solution may have a softening and tenderizing effect upon cooked meat products. For
example, beef patties containing 1.0% HPMC were evaluated by a sensory panel to have
increased tenderness (Hill and Prusa 1988). Softening and tenderizing trends with the
addition of 0.5 or 1.0 % MC to beef rolls was also reported by Shand and others (1993).

However, increased softness values are not desirable in restructured meat products.

99

EBA: 68%? 82 m2
.czm—mv emu—2 2: mo Sum 23.8% _
£05885; 83a 3. 05 $5 326653, 8% .L 05 wﬁhﬁ «Ba 05.? cum.— oﬁ ﬂ oocoﬁmox ._
.mmoﬁwﬁam*mmo:o>_monou*mmo:v§: .«o 8.605 2: m_ $05320.
.A_<\m<v =o_mmoEEOo “we 05 wESc «m5 3 863528 EN 2: 9:56 no.8 02$ 0338a mo 0:8 05 mm $0533.33
.:o_mmo.&88 vacuum 28 “mum 05 :83qu £308.. team 05 Ems: 05 mm mmoﬁwctam a
.va Emma? 2953 \ seamen—Boo “we wESw 080m xmoa 05 ﬂ 3263: m
.Egotﬂm ban >23; a can 82a 58 mm 53 93— mg m a maﬁa gimp—@800 293 -N ”mix—m5 oan 95:83
.385 32: 2a 8:28 2.3 2 32; 25 22.8an .8 §§ a. to 5.8 .23 o
.2: 580582 H. 08383506
38:35:23 .Zw/x EamUOIHmE ; owe—2.33505 630 m: ©=tm£oO uncoowmhmo 258. ”09; 22.8233 a
Amodvnc =5be baa—mommawﬁ 2m £52 £55, mitomhomsm 32056 wags: 2802 9a

 

 

:3 ammo ammo 3.5 a; “one x8§=$m
Sam £38 “29: €932 93$. 2.th _ 3 $0555
:3 $2 “85 no; :2 no; _aocozmoﬁu
_.o 3 _._ 2 mo 2 232.5 aogwsam
a: 29%. ~32 g3: 09% 23; _ E33 33 30%;:
..ou—ﬂuoh

35 9o \ 9o \ to 3 \ 9o 3. \ to 3 \ to 3 ..33

 

0v:— DSEE— DE 0!: USE: Uvs DE — DEE DE .2230

 

.393. 32.895»:

 

...—89mm :3:— EEE a E 355 29:39.??—
? 2222.583 an???» 5.3 3..-53.3.3:— Ea: 3..—59:53.. .3 <9“. ...: ago:— ouaswm aged 6 033—.

100

Restructured products with high amounts of added water can lose textural integrity;
consequently, increased hardness values are desired (Shand and others 1994).
Springiness and cohesiveness values were the highest for the CONT and the lowest for
TRT 1 (Table 6). These results demonstrate that TRTs containing MC and/or HPMC are
less likely to spring back to normal size and bind as a cohesive unit. This suggests that
MC and/or HPMC will result in a softer, looser bound end product. Chewiness values
ranged from 396.3 to 1495.2 g/sample with TRT 3 being the chewiest and TRT 1 have
the least amount of chewiness (Table 6). The CONT tended to have the highest amount
of resilience with TRT 1 having least. These results suggest that the addition of MC
and/or HPMC may promote a softening effect in restructured ham products that makes
them less resilient, less springy, and less cohesive as the CONT. However, these results
may also be due to the increased binding of water compared to the CONT resulting in the
textural attributes recorded.
Conclusions

The ability of MC I and/or HPMC I with KC to increase water binding and
retention while maintaining ham quality was demonstrated in Experiment IV. The data
suggest there may be a potential synergistic effect between MC I and/or HPMC I with
KC. More research is needed to determine synergistic effects as this study was not
designed to determine synergistic effects. This can be done by a statistically planned
study. Overall, high-moisture restructured ham in Experiment IV had higher cook yields
and lower purge values when compared to the Experiment III. However, when MC 1 and
HPMC I were utilized singularly in a meat system (Experiment HI) they performed as

previous studies had suggested. Hill and Prusa (1988) and F oegeding and Ramsey (1986)

101

both determined at the use of METHOCELTM signiﬁcantly decreases water binding
abilities.

Study I determined that the use of varying combination hydrocolloid brine
solutions in a high-moisture restructured ham (Experiment IV) has purge controlling
attributes. Although this study was performed bench top, there is still sizeable evidence
that these combination treatments (Experiment IV) will be an advantage in commercial
ham production. These formulations will be scaled up and issues will be addressed in

study II concluding with a trained sensory panel.

102

References

Anonymous. 2000. Product selection guide for METHOCELTM food gums. The Dow
Chemical Company.

Anonymous. 2001. A food technologist's guide to METHOCELTM food gums. The Dow
Chemical Company.

Daniel, JR, Weaver, CM. 2000. Carbohydrates: Functional properties. In: Christen, GL,
Smith, J S. Food Chemistry: Principles and Applications. West Sacramento, CA: Science
Technology System. P 55-77.

DeFreitas, Z, Sebranek, JG, Olson, DG, Carr, JM. 1997. Freeze/thaw stability of cooked
pork sausage as affected by salt, phosphate, pH, and carrageenan. J Food Sci 62(3):551-
554.

Dutson, TR. 1983. The measurement of pH in muscle and its importance to meat
quality. Reciprocal Meats Conference Proceedings 36:92.

F oegeding, EA, Ramsey, SR. 1986. Effect of gums on low-fat meat batters. J Food Sci
51:33-35, 46.

Grover, JA. 1986. Food Hydrocolloids, Vol III. Glicksman, M, editor. Boca Raton, FL:
CRC Press Inc. P 121-154.

Hamm, R. 1994. The inﬂuence of pH on the protein net charge in the myoﬁbrillar
system. Reciprocal Meat Conference Proceedings 47:5-9.

Hill, SE, Prusa, KJ. 1988. Physical and sensory properties of lean ground beef patties
containing methylcellulose and hydroxypropyl methylcellulose. J Food Qua] 11:331-337.

Miller, R. 2000. Functionality of non-meat ingredients used in enhanced pork. In:
National Pork Board Pork Quality Facts. Des Moines: IA. P 1-10.

Mittal, GS. Barbut, S. 1993. Effects of various cellulose gums on the quality parameters
of low-fat breakfast sausages. Meat Sci 35:93-103.

Osburn, WN. 2001. Graduate course: FSC 433-Food Processing: Muscle Foods.
Michigan State University, East Lansing, MI.

Pearson, AM, Gillett, TA. 1996. Introduction to meat processing, raw materials;
sectioned and formed meat products; sausages; casings, extenders, and additives.
Processed Meats, 3rd Edition. New York, NY. P 1-22, 126-143, 144-179, 210-241, 291-
3 10.

103

Prabhu, GA, Sebranek, JG. 1997. Quality characteristics of ham formulated with
modiﬁed corn starch and kappa carrageenan. J Food Sci 62(2): 198-202.

Priya, R, Singhal, RS, Kulkami, PR. 1996. Carboxymethylcellulose and hydroxypropyl
methylcellulose as additives in reduction of oil content in batter based deep-fat fried
boondis. Carb Poly 29:333-335.

SAS Institute, Inc. 2002. SAS User’s Guide, Version 8.2. Cary, NC: SAS Institute.

Shand, PJ, Sofos, JN, Schmidt, GR. 1993. Properties of algin/calcium and salt/phosphate
structured beef rolls with added gums. J Food Sci 58(6): 1224-1230.

Shand, PJ, Sofos, JN, Schmidt, GR. 1994. Kappa-carrageenan, sodium chloride, and
temperature affect yield and texture of structured beef rolls. J Food Sci 59(2):282-287.

Steinke, LW. 2001. Moisture management and texture enhancement in chicken patties
containing methylcellulose [MS thesis] East Lansing. MI: Michigan State University. 123
p. Available from: Michigan State University.

Trius, A, Sebranek, JG, Rust. RE. Carr, J M. 1994b. Carrageenans in beaker sausage as
affected by pH and sodium tripolyphosphate. J Food Sci 59(5):946-951.

Trius, A, Sebranek, JG. 1996. Carrageenans and their use in meat products. Crit Rev
Food Sci Nutr 36(1-2):69-85.

Trudso, JE. 1985. Increasing yields with carrageenan. Meat Processing 24(2):37-42.

104

CHAPTER 4

EVALUATION OF HYDROCOLLOID INGREDIENTS AS PURGE
CONTROLLERS IN HIGH-MOISTURE RESTRUCTURED HAM

ABSTRACT

Hydrocolloid brine solutions were formulated using methylcellulose (MC),
hydroxypropyl methylcellulose (HPMC) and kappa carrageenan (KC): 1) MC 0.4% &
KC 0.6%; 2) HPMC 0.6% & KC 0.6%; 3) MC 0.4% & HPMC 0.6% & KC 0.6%; 4) KC
0.6%; 5) Control: no hydrocolloids, and evaluated as purge controllers. TRTs (45%
addition wt/w ) were mixed into a restructured ham formulation ground and thermally
processed to 70°C. TRT l and 3 increased (P<0.05) cook yields and decreased purge
values by >1.5%. TRT 1, 2, and 3 improved ham exterior and interior L* surface values
and textural values. TRTs containing MC and/or HPMC with KC may control purge and

maintain product quality attributes.

*This chapter is formatted in manuscript style according to the Journal of Food Science.*

Key Words: hydrocolloids, purge controllers, restructured ham

105

Introduction

As the amount of added water in high-moisture (>45% addition) restructured ham
increases, the ability to retain water during thermal processing and minimize purge
during storage decreases (Prabhu and Sebranek 1997). With the addition of non-meat
ingredients such as binders, extenders. or purge controllers, increased water binding and
retention has been documented. Kappa carrageenan (KC) is a purge controlling
hydrocolloid that is readily utilized, industry-accepted, and processor-friendly. Previous
studies have shown that the addition of 0.5% KC improves cook yield, decreases purge
values, and improves Sliceability in cured turkey breast and turkey ham sectioned and
formed products (Bater and others 1992; Bater and others 1993). Shand and others
(1994) utilized 0.5 and 1.0% KC in lean structured beef rolls resulting in improved
texture, increased water retention, and decreased purge. Additionally, 0.5% KC was
incorporated into cooked pork sausage to effectively decrease ﬁ'eeze/thaw purge values
(DeFreitas and others 1997). Bater and others (1993) also found that the addition of
0.5% KC decreased freeze/thaw purge values by 1.5% in cured ham-like turkey product.

The incorporation of methylcellulose (MC) and hydroxypropyl methylcellulose
(HPMC) may also enhance restructured product tenderness and juiciness. The utilization
of MC and/or HPMC may enable the meat processor to further use lower quality, tough
meat cuts with more connective tissue due to their tenderizing ability. Hill and Prusa
(1988) noted the addition of 1% HPMC to lean ground beef patties increased tenderness
and juiciness when compared to the control. Shand and others (1993) also saw a

signiﬁcant decrease in hardness values for structured beef rolls with 0.5 and 1.0% MC.

106

Chicken patties with 0.25 and 0.5% MC were more tender and juicy when compared to
the control (Steinke 2001 ).

The combining of MC and/or HPMC with KC may provide a potential synergistic
effect when incorporated into meat products as a brine solution, thereby promoting water
binding and retention during thermal processing and subsequent storage. Utilizing
hydrocolloid gums that gel upon thermal processing (MC and HPMC) with KC that gels
upon cooling following thermal processing may entrap added water during the cooking
and cooling process. Additionally, phosphates within the brine solution will contribute to
water holding capacity and ﬂavor enhancement (Barbut and others 1988; Matlock and
others 1984; Keeton and others 1984), while salt improves WHC, cooked color scores,
and sensory attributes (Schwartz and Mandigo 1976). However, further research is
necessary to determine if MC and/or HPMC with KC exhibit a synergistic purge
controlling effect in high-moisture restructured ham. The hypothesis was high-moisture
restructured ham manufactured with varying combinations of hydrocolloids (MC,
HPMC, KC) can control purge without detrimental effects on textural and sensory
attributes.

The speciﬁc objective of this study was to investigate the effects of incorporating
hydrocolloid brine solutions into a high-moisture (45% added water) restructured ham

product on cook yield, purge, and quality attributes.

107

Materials and Methods

Preliminary Study
A preliminary study was conducted to confirm Study I results in a pilot plant

setting. The hydrocolloid brine solutions from Experiment IV (Study I) and three control
hydrocolloid brine solutions were used to manufacture added water (45% wt/wt)
restructured hams. Hydrocolloid (A4M: MC 1; F4M: HPMC I; KC; Control: no
hydrocolloids) brine solution treatments (TRT) formulated were:

TRT 1 — 0.4% MC Ix 0.6% HPMC I

TRT 2 — 0.4% MC Ix 0.6% KC

TRT 3 — 0.6% HPMC Ix 0.6% KC

TRT 4 — 0.4% MC I x 0.6% HPMC Ix 0.6% KC

TRT 5 - Control

TRT 6 — 0.4% MC I

TRT 7 — 0.4% HPMC I

TRT 8 — 0.6% KC
Ground ham muscle (5.7 kg) and 2.6 kg of either a hydrocolloid or control brine (45%
addition) solution were mixed together for 10 min in a modiﬁed double axel paddle mixer
(Model T-268, Keebler Engineering Inc., Chicago, IL). Mixed restructured ham batter
was placed into a vacuum stuffer (Model 500, VEMAG Maschinenbau GmbH,
Germany), stuffed into pre-soaked 11.4 cm x 76.2 cm ﬁbrous, non-perforated, preclipped
casings (Devro-Teepak, Inc., Kansas City, MO.), and clipped using a Tipper Tie Clipper

(Model PR465L, Dover Industries Co., Aspex, NC). Restructured hams were thermally

108

processed to an internal temperature of 70°C utilizing a one truck smokehouse (CGI
Processing, Model A28- B0101, Automated Manufacturing, Cicero, IL). Thermally
processed restructured hams were placed into a 2-4°C cooked meat cooler and chilled to
4°C for approximately 16 hrs according to Appendix B guidelines (USDA-FSIS). All
restructured ham treatments were subjectively evaluated for casing peelability, ham
ﬁrmness, Sliceability, and cook yield. Restructured ham formulations that exhibited poor
cook yields, Sliceability and/or soft texture were eliminated from further investigation.
Acceptable restructured hams were formulated from TRT 2, 3, 4, 5, and 8. These hams

were sliced (1.27 cm), vacuum packaged and stored (2°C) for sensory panel training.

Experimental Design and Data Analysis

The experimental design for this study was a one-way ANOVA with three
treatment combinations (0.4% MC I/0.6% KC, 0.6% HPMC I/0.6% KC, 0.4% MC
I/0.6% HPMC I/0.6% KC) at 45% addition (wt/wt), with a hydrocolloid brine control
(KC at 0.6 %; 45% addition WM) and a control (no hydrocolloid; 45% addition, wt/wt).
Main effect means were separated by Tukey's Honest Signiﬁcant Difference test with a
predetermined level of signiﬁcance (P<0.05) (SAS user’s guide, version 8.2. Cary, NC:
SAS Institute, Inc., 2002).
Hydrocolloid Ingredients

The hydrocolloid ingredients were described previously in Chapter 3.

Manufacturing Process

A. Brine Manufacturing

109

Three multi-hydrocolloid brine solutions, 3 KC, and a control brine solutions were
prepared for each replication for each treatment group (Appendix 9). Each brine solution
was formulated prior to each restructured ham production day. The formulated treatment
brine solutions were:

Treatment 1 — 0.4% MC I x 0.6% KC

Treatment 2 — 0.6% HPMC I x 0.6% KC

Treatment 3 — 0.4% MC I x 0.6% HPMC Ix 0.6% KC
Treatment 4 — 0.6% KC

Treatment 5 — Control

Treatment brine solutions (11.4 kg) were placed in plastic containers and mixed
using a Rotostat mixer (Model 80XP63SS, Admix Inc., Londonderry, NH) modiﬁed by
Michigan State University at 1200 rpm during the addition of phosphate, salt, and sugar.
During the addition of the hydrocolloid gum(s) mixing speed was increased to 1500 rpm
to fully entrain hydrocolloid. Total mixing time was 20 minutes per brine. The brines
were covered and placed in a 2°C cooler for 12-16 hrs. Upon completion of storage (12-
16 hrs), brines were remixed for 1 minute at 1200 rpm. Nitrite and erythorbate were then
added and mixed for an additional 2 minutes at 1200 rpm.

B. Restructured Ham Processing

Fresh, boneless, semimembranosus muscle (IMPS 402F), with the gracilis muscle
on, was acquired from a local meat company. Ham muscles were randomly selected and
trimmed to remove the gracilis muscle and external fat. The ham muscles were weighed

according to the appropriate product formulation, placed in plastic meat lugs and covered

with SaranTM wrap.

110

Fresh pork semimembranosus muscles (gracilis muscle removed) were sorted in
5.7 kg batches per restructured ham treatment. The ham muscles were further divided
into three 1.9 kg batches for grinding into three different particle sizes (Prabhu and
Sebranek 1997). One 1.9 kg batch was ground through a 5.33 cm plate (kidney plate),
the second batch was ground through 2.54 cm plate and the last batch was ground
through a 0.95 cm plate (TORREY Grinder Model M-32-5, Maquinas Para Mercados,
S.A. DE C.V., Mexico). The ground ham muscles (5.7 kg, 1.9 kg of each particle size)
and 2.6 kg of either a hydrocolloid or control brine (45% addition) solution (Appendix 9)
were placed into a modiﬁed double axel paddle mixer (Model T-268, Keebler
Engineering Inc., Chicago, IL) and mixed for 10 min. Upon completion of mixing, a
sample for raw proximate analysis and pH determination were collected. Mixed
restructured ham batter was placed into a vacuum stuffer (Model 500, VEMAG
Maschinenbau GmbH, Germany), stuffed into pre-soaked 11.4 cm x 76.2 cm ﬁbrous,
non-perforated, preclipped casing (Devro—Teepak, Inc., Kansas City, MO.), and clipped
using a Tipper Tie Clipper (Model PR465L, Dover Industries Co., Apex, NC). Stuffed
and clipped ham chubs were weighed and recorded as a treatment group. Restructured
ham chubs were hung on smoke sticks and placed on a smoke truck for thermal
processing.

C. Thermal Processing
Thermal processing was achieved utilizing a one truck smokehouse (CGI

Processing, Model A28- B0101, Automated Manufacturing, Cicero, IL) to an internal

temperature of 70°C (Table 7).

111

Table 7: Smokehouse Schedule

 

 

Time Internal Dry Bulb Wet Bulb

Stage (Min) (°C) Smoke (°C) (°C) Fan Damper

1 15 0 no 43.3 37.8 50 Open

2 30 0 no 54.4 43.3 50 Open

3 30 0 no 60.0 46.1 50 Open

4 30 0 no 65.6 48.9 50 Open

5 45 62.8 no 71.1 54.4 50 Open

6 120 62.8 no 71.] 62.8 50 Open

7 240 70.0 Steam 79.4 71.1 50 Open
Shower 30 54.4 No 1 min on 1 min off 100 Closed

 

Following the shower cycle, the restructured hams were removed ﬁ'om smokehouse once
an internal product temperature of 54.4°C was reached. The restructured hams were
allowed to equilibrate to an internal temperature of 378°C (30 min) at 20°C. Excess
water was removed and the treated products were weighed to determine product cook
yields (3 78°C). The restructured hams were then allowed to equilibrate to an internal
temperature of 322°C (15 min) at 20°C prior to chilling.
D. Chilling, Slicing, and Packaging Process

Thermally processed restructured hams were placed into a 2-4°C cooked meat
cooler and chilled for approximately 16 hours to an internal temperature 24°C according
to Appendix B guidelines (USDA-FSIS). Casings were then removed from barns and
discarded.

Three restructured ham chubs per treatment were sliced into 1.27 cm thick slices
using a Globe meat slicer (Model 775L, Mozley Mfg. Co. Inc., Stamford, CN).
Restructured ham slices were randomly selected and vacuum packaged. Two slices were

packaged for cooked proximate composition and pH determination and stored in a -

112

288°C freezer. Twelve randomly selected ham slices were vacuum packaged (30.5 cm x
35.6 cm bags) (Cryovac Sealed Air Corp., Duncan, SC) for trained sensory panel
evaluation. One ham slice was randomly selected for day 0 lipid oxidation analysis,
packaged and heat sealed (Diagger, Lincolnshire, IL). Four ham slices were randomly
selected for textural analysis - two for objective texture proﬁle analysis and two slices for
Kramer Shear analysis then packaged into 17.8 cm x 30.5 cm bags. Twenty ham slices
were randomly selected for color, purge, and lipid oxidation analyses; 4 slices per day, 2
slices per bag (17.8 cm x 30.5 cm), 2 bags per treatment for evaluation on day 7, 14, 21,
28, and day 56 of refrigerated (4°C) storage. All vacuum packaged samples were
packaged using a Multivac vacuum packager (AGW, SeppHaggenmuller KG, Germany)
with a vacuum setting of 2.5 vacuum and a heat sealer bar setting of 3.0.
Restructured Ham Storage

Vacuum packaged restructured ham slices were placed in a 4°C, walk-in cooler.
Packages were laid ﬂat, non-overlapping on white plastic trays which were placed on
tables 2.08 meters from a constant light source. The cooler contained 10 lighting ﬁxtures
and 2 ﬂuorescent lamps (Model F4OSP41, General Electric, Cleveland, OH) per ﬁxture
(n=20). Lighting was monitored everyday for a total of 56 days, burnt lamps were
changed as needed and remained on throughout the study. F oot-candle (F C) readings
(F C=80) were taken using a GE Triple Range Light Meter (Model 217, General Electric,
Cleveland, OH) from the surface of the ham slice. The foot-candle reading (FC =80) is

equivalent to 24,407 lumens.

Analyses

113

A. Hydrocolloid Brine solution and product pH Determination
Brine solution and raw and cooked restructured ham pH values analyses were
determined as previously described in Chapter 3.
B. Product Cook Yield Determination
Cooked product yield was determined as previously described in Chapter 3.
C. Color Analysis, TBA analysis and Purge loss
Objective color determinations for the exterior ham surface (exposed to light) and
the interior ham surface (unexposed to light) was measured using a Minolta Chromameter
(Model CR-310, Minolta Camera Co., Ramsey, NJ). Three readings were taken and
averaged for L* (lightness), a* (redness), and b* (yellowness) values (Commission
Internationale De L’Eclairage (CIE)). The Chromameter was set on D65 illuminant
(daylight illuminator), 2° standard observer, with a 50 mm reading oriﬁce. The
Chromameter was calibrated on a standard white and the pink color tile. Color readings
were taken for day 0, 7, 14, 21, and 28.
Thiobarbituric acid reactive substance (TBARS) analysis was conducted on day 0,
14, 28, and day 56, to monitor oxidative rancidity. Four replicates were run for each
sample according to methods established by Tarladgis and others (1960) and Zipser and
others (1962) as modiﬁed by Rhee (1978). Percent purge was determined for days 7,
14, 21, 28, and day 56 of refrigerated (4°C storage) as previously described in Chapter 3.
Proximate Composition
Moisture (oven drying), fat (Soxhlet ether extraction), and protein (nitrogen
measurement, Model FP-2000, LECO Co., St. Joseph, MO) were determined according

to AOAC (2000) methods. Samples were analyzed in triplicate.

114

T extural Analyses
A. Texture Proﬁle Analysis (T PA) :2-cycle Compression

Restructured ham slices were analyzed using the 2-cycle compression test
method, utilizing a TA-HDi Texture Analyzer (Texture Technologies Corporation,
Scarsdale, NY). Two restructured ham slices per treatment were removed from vacuum
packaged bags and held at 4°C. Two circular samples 1.9 cm diameter x 1.3 cm thick,
were cut from the center from each ham slice. Each treatment was analyzed in
quadruplicate. A 5 kg load cell was used to measure hardness, springiness, cohesiveness,
chewiness, and resilience using a 75 mm diameter aluminum cylinder plate (TA-30), on a
heavy duty platform (TA-90). Samples were compressed to 25% of original height (75%
compression) in a 2-cycle compression at 4-6°C with a crosshead speed of 1.7 mm/s.

B. Kramer Shear Force Determination

Restructured ham slices were analyzed using the Kramer 5-blade shear force test
method, utilizing a TA-HDi Texture Analyzer (Texture Technologies Corporation,
Scarsdale, NY). Two restructured ham slices per treatment were removed from vacuum
packaging and covered to prevent surface drying at 4°C. A rectangular sample measuring
7.9 cm x 6.4 cm x 1.3 cm was cut from the center of each ham slice using a pre-made
plastic template. A 50 kg load cell with a crosshead speed of 1.7 mm/s was used to
measure peak force in Newtons (N) required to shear the restructured ham slice.
Trained Sensory Panel Evaluation

A trained sensory panel (n=6)was utilized to determine speciﬁc sensory attributes

of each restructured ham product. The panel was trained according to AMSA (1995) and

115

Meilgaard and others (1991). Each restructured ham treatment was evaluated using 8
point hedonic scale where 1=extremely soft and 8=extremely hard, l=extremely dry and
8=extremely juicy, l=no residue/mouth coating and 8=abundant residue/mouth coating,
l=no off-ﬂavor detected and 8=abundant off-ﬂavor. Samples were prepared by cutting
1.27 cm3 cubes from the center portion of each ham slice and were served cold (4-6°C).
To minimize positional bias, the order of sample preparation was randomized within each
session (Meilgaard and others 1991).

Testing took place in climate controlled, partitioned booths with cool
incandescent light. Three cubes were placed in a plastic custard dish and held, covered to
prevent surface drying in a 4°C cooling unit until served. Each sample was served to
panelists through a vertical sliding door that separated the food preparation area from the
sensory testing area. Panelists were instructed to handle sample cubes with supplied
wooden toothpicks, and tasted for hardness, juiciness, residue/mouth coating, and off-
ﬂavor intensity. Expectorant cups were provided to prevent taste fatigue as the panelists
were instructed not to swallow the samples. Distilled, deionized water and unsalted soda
crackers were used to clean the palate between samples. Fifteen (4 treatments, 1 control
and 3 replications) samples were evaluated in one day. The day was divided into 3
sessions with 5 samples evaluated per session. The panelists were standardized for each
session by evaluating l warm-up sample and discussing the results. The warm-up
samples were either the control or the KC treatment. There was 5 minutes between each

sample and a 15 minute break between sessions.

116

Results and Discussion

Differences (P<0.05) between treatments were observed for cook yield, textural
measurements (TPA and Kramer shear), sensory attributes and proximate composition.
No signiﬁcant (P<0.05) treatment by day interactions for purge, lipid oxidation, and color
(L*, a*, b*) were seen from day 0-56. Signiﬁcant main effect differences (P<0.05)
between day of storage (7-56) were also observed for purge loss, lipid oxidation and
color (L*, a*, and b*). No signiﬁcant main effect differences between treatments
(P>0.05) were observed for brine pH, restructured ham raw pH, cooked pH, and raw
batter % fat proximate composition. No main effect differences (P>0.05) were seen
between storage days for color (L*, a*, and b*). Treatments (TRT) within this study will
be referenced as follows: TRT 1: MC I/KC at 0.4/0.6%, TRT 2: HPMC I/KC at 0.6/0.6%;
TRT 3: MC I/I-IPMC I/KC at 0.4/0.6/0.6%, TRT 4: KC at 0.6%, and TRT 5: the control
brine: no hydrocolloid.

Brine pH measurements between treatments ranged from 7.27 to 7.43 (Table 8).
Treatment 1 had the highest brine pH value and TRT 4 the lowest. Restructured ham raw
pH values ranged from 6.42 to 6.47 and cooked ham pH values ranged from 6.50 to 6.53.
No diﬂ‘erences in pH (brine, raw ham, cooked ham) due to treatments were observed.

Treatment 5 raw restructured ham moisture was the highest and TRT 1 had the
lowest % moisture content (raw) (Table 8). Raw percent fat values ranged from 1.3 to
1.4%. Raw ham protein content values were the highest for TRT 1 and the lowest for
TRT 4. The dilution of meat protein is due to 45% brine addition. Cooked ham percent
Moisture content varied by more than 3% between TRTs. TRT 4 had the highest cooked

moisture composition at 77.0%, 2% higher than the other treatments within the study and

117

Table 8: Least square means for pH and proximate composition of high-moisture
restructured ham manufactured with varying combinations of

hydrocolloid brines.

 

 

 

 

 

Hydrocolloid Typed
Treatment‘3 1 2 3 4 5
MC I/KC HPMC [IKC MC l/HPMC I/KC KC Control
Levelf 0.4 / 0.6 0.6 / 0.6 0.4 / 0.6 / 0.6 0.6 0.0 SEM"
Brine p118 ”5 7.43 7.37 7.40 7.27 7.30 0.07
Raw pH” ”3 6.47 6.45 6.47 6.43 6.42 0.01
Cooked pHi “5 6.52 6.53 6.53 6.52 6.50 0.01
Proximate
Composition‘
Raw
% Moisture 79.2c 80.5”c 80.0”c 81.3”” 82.0” 0.4
% FatNS 1.4 1.3 1.4 1.3 1.4 0.1
% Protein 16.5a 15.4”” 155*” 15.1” 16.0“” 0.3
Cooked
% Moisture 75.7a 73.3” 73.2” 77.08 75.38” 0.5
% Fat 1.6” 2.3”” 2.1:” 2.2”b 2.5” 0.2
% Protein 20.5”c 22.5' 22.3' 19.5”- 21.3‘” 0.4

 

°'° Means having different superscripts within rows are signiﬁcantly different (p<0.05).

d Hydrocolloid Type: kappa carrageenan Gelcarin® ME 6910, methylcellulose I: METHOCELTM
A4M, hydroxypropyl methylcellulose I: METHOCELTM F4M.

cTreatment identiﬁcation of brine solution.

f Level (0.0, 0.4 & 0.6%) of hydrocolloid type added to brine solution and meat model.

3 pH measurement of brine at 5°C.

h pH measurement of raw ham samples at 4°C, 1 week post-processing.

pr measurement of cooked ham samples at 4°C, 1 week post-processing.

JProximate Composition: Percent moisture, fat, and protein of raw and cooked high-moisture
restructured ham samples. -

" Standard error of the mean (SEM).

”5 Not signiﬁcant (P>0.05)

118

signiﬁcantly higher than TRT 2 and 3. These results are supported by higher cooked
product moisture content (76-78%) in structured beef rolls with 0.5 and 1.0% KC (Shand
others 1994). Bater and others (1992) utilizing 0.5% KC in roasted turkey breast also
demonstrated higher percent moisture values when compared to the control. Numerically
TRT 4 raw and cooked restructured ham samples consistently recorded the highest
percent moisture content and the lowest percent protein composition.

Cook yield values between the treatments ranged from 83.1 to 91.6% (Table 9).
TRTs 1 and 3 had the highest cook yield values at 91.9 and 91.6% respectively,
signiﬁcantly higher than TRT 2 and 5. TRT 5 had the lowest cook yield value at 86.1%
and TRT 2 was similar to TRT 5 at 83.2%. TRTs 1 and 3 may be demonstrating a
synergistic or additive effect between MC I and KC that allows for increased water
binding. Numerous studies have shown that utilizing MC or HPMC singularly will
signiﬁcantly decrease moisture retention (Foegeding and Ramsey 1986; Hill and Prusa
1988; Shand and others 1993; Mittal and Barbut 1993). The decrease in cook yields due
to the addition of MC and HPMC was also shown in Study 1, Experiment III. However,
there is no previous research combining MC and/ or HPMC with KC to substantiate these
cook yield results. Chicken patties with 0.25% MC had a signiﬁcantly higher cook yield
value (75.58%) when compared to the control (74.66%) (Steinke 2001).

Purge values between treatment ranged from 4.3 to 0.9% and storage day purge
values ranged from 2.0 to 2.5% (Table 9). TRT 2 had the lowest purge value at 0.90%, a
3.4% greater (P<0.05) purge reduction when compared to TRT 5 (4.3%) and greater than
1.9% purge reduction when compared to TRT 4 (2.8%). Increasing length of storage

suggested an increase in purge values. Day 56 storage was the highest in purge loss

119

.Azmmv :88 05 go She Eng—Sm o.
em. 25 mm .3 .o be so one
€258: com 2958 En: 356332 mo wococ302m=035 we means—«>0 68 $05333 2532 Eon ecu—“Eamnomﬁrm u max}:H
.3303 EB + 295$ owmxomm 038$. _38 \ .3, was 5 + S, 295% it H 09.5 .x...
.Uoon 8 36.08 £52 uocsaoaumom .2: ...Ewmok 335363 ©8300 "20$ x80 .x. A
.EvoE 32: use cots—em 05.5 3 new?“ 25 20:08:33 mo ¢§©d a. v.0 6.8 .33 m
28:28 onto me cosmoEEQE “5836:. a
SE 2:30:52 ; o8_e=oo_§oe

_Eenﬁxocwm: .2v< seam—003932 a 322—8352: 630 £2 @53200 35%th 893— 593. 22.808»: 6
Amodvnc acoaoﬁmw 323$ch as 958 £53, manomcoazm “schemata wage; memo—2 e-“

 

 

 

 

 

 

 

3.0 L _.o eeo _ .c - L ﬁo . ewod Sod mod Sod :od mod ..mﬁmh
_.o .2 2; .__.~ 3.3 33 - L m... .62 _._? .53 .2; _owsm .x.
6.0 .2 .8 no.8 .e. a .2» .6. a £26; U_eeo .x.

32mm on mm _m E n c od ed ed \ ed \ to cd \ 06 9o \ «6 “—301—
nﬁaa .235 u: 85 92.5: oz 85 02mm 85 u:
m w m N _ mac—5.3.5.
ocean. 22.395»:

 

.353 22.396»: no 253.3388 ugh—a.» 5.? 62:88:55
Ea.— uoaaosbmoa 95338-53 no 23m :89 2.3.89 ES .owasn 2.3.3; .mﬁmh .5.— ..anE 9:33 «muon— um 03.;

120

while day 7 was the lowest. TRT 4 purge values are similar to high-moisture ham
manufactured with 1.5% KC in. a study conducted by Prabhu and Sebranek (1997).
Shand and others (1994) also had a signiﬁcant decrease in purge values by 2.2 and 1.6%
when utilizing KC at 0.5 and 1.0% in structured beef rolls when compared to the control
(10% purge). TRTs 1, 2, and 3 were the most effective at decreasing purge loss.
Treatment 1 combined the highest cook yield value (91.9%) with a purge loss value of
1.5%. These values are signiﬁcantly higher than TRT 5. This is a decrease of purge by
2.8% when compared to the TRT 5 and a decrease of 1.3% when compared to TRT 4.
These decreases in water loss are of special interest from an industry perspective. Over
time decreasing purge by 2.8% and increasing cook yields by 5.8% may create proﬁtable
revenues for the meat processor. Additionally, the increase in water retention and
binding can also be beneﬁcial to the consumer as it would potentially decrease product
cost at the retail case. The binding of more water could also provide a product that is
blander in ﬂavor, lower in calories, and more appealing to a wider consumer population.

Lipid oxidation (TBARS) values ranged from 0.08 to 0.114 for all treatment and
storage days indicating very little lipid oxidation (Table 9). No differences between
treatments were signiﬁcant (P>0.05). Days 14 and 56 had the highest TBARS values
while day 0 TBARS analyses were the lowest. Although, there was a difference between
days this difference is not of practical signiﬁcance.

Color was analyzed on the exposed and unexposed surfaces of the ham samples.
There were signiﬁcant differences (P<0.05) between treatments for lightness (L*),
redness (b*), and yellowness (a*) on the exposed and unexposed ham slice surfaces

(Table 10). These variations in color may be due to the inconsistency of the ham slice

121

surface. Prior to restructuring, inside ham muscles were ground to 3 different particle
sizes (5.33 cm, 2.54 cm and 0.95 cm). This creates a very non homogenous surface area
compared to the homogeneity that would be seen in frankfurters and other emulsiﬁed
products. During color analysis, ham slice would be expected to vary in the portion of
particle sizes displayed in the exterior and interior surfaces of each individual ham slice,
resulting in variation of color measurements. Lightness (L*) measurements for TRT 2
exposed and unexposed ham surfaces were lower compared to other treatments (Table
10). TRTs 4 and 5 tended to have the lightest colored ham samples for both the exposed
and unexposed readings. Mittal and Barbut (1993) reported that low-fat cooked breakfast
sausage containing 1% carboxymethyl cellulose decreased L* values compared to low-fat
breakfast sausage containing no hydrocolloid gums. Steinke (2001) also found chicken
patties with 0.25 and 0.50% MC resulted in a lighter colored product. Steinke’s (2001)
ﬁndings contradict L* results seen within this study.

Lightness measurements between storage days (0-28) were different (P<0.05) for
unexposed areas (Table 10). Numerically, day 0 reported the highest L* values between
days. Overall, TRTs 1, 2, and 3 exhibit an ability to sustain acceptable cured meat color
over storage time. This is a valuable attribute since ham with 45% added water is
initially lighter in color. Redness (a*) values for TRT 3 samples were redder in color for
exposed and unexposed a* values than the other treatments. These results also suggest
future research needs to be conducted to identify the reasoning for why TRT 1, 2, and 3
retain more redness (a*) when compared to TRT 4 and 5. TRT 4 tended to have lower
redness values when compared all remaining TRTs. Generally, as the length of storage

increased, redness values increased for both the exposed and unexposed surfaces.

122

.956 5.2.. 2.. ... 88 285% _

Am-.. 22532 on. .8 8.00 8&2; 38:55. 28 3898 50253 8055...“... 2203.. BSA—mam 3.85:8... 0.8 68.53. 32.3 ._

AmodAmv 2.85%? 8: Pa matomsgm :55? 83.3 "ml.

3.08.5.8 80.8.00 a $.35: Dov ... 38...; @8033: E... .

33.70 2: cc 8153 :8: 3.30.58. .0838 .6 $3 30:50:...» 5.3 $260.. 5...: 35.8%.. ”Ammo. 33.3094 00 03:22.88:— =e_mm_EEoUv .200.
.08... .8... ...... 8.3.... 8.... o. 3...... 2.... 2268...... .... £0... ... 2. ....8 .25. .

muons—cm 055 he 5.30.0552 0.8.58.5. m

.2... 5500582 N. 0.223236... .2832... .23.. 360058). N. 822.8352: .28 m2 @5328 550.350 2...... .25 2238...... .

.Amodvnv BENCE 3.565%? 0.8 m3... 553» 995309.... 2.0.8.06 wig: £802 .1.

 

 

 

 

 

123

...... NM... ..N... N... 3... ON... ..NN... ...N... .3... ..N... .2... 855:5...
2.... ..n... ...N... .2... .9... ...... ...: .8... .8.“ .8... .2... .. 8.3.8:
...... «N... ON... NN... 9N... ...... .8... .2...“ ...... .NS. ...? .3886
.... ...... .2. ...... .2. .2. N... ...... c... o... 0... 8.5.0.05 ...
.... .N... ...... .9... .N... .2. EN... ...... ...... ...... ...... .. 88%....
.... .3. ...... ...... ...... ...: ...... ...... ...... .....N. ...... Essa...
N... S N.. .... .... ... N.. .... ... .... ... .8535...
no ...... ...... ..Né ...... ...... ...... ..N... .2... .20 .2... .. 889...:
N... ...... 2.. ...... N... ...... ...... .N... .33 .2. ..N... ......axm
.330 ouauusw
.25 ..N .N ... N o o... o... o... \ o... \ ...o o... \ o... o... \ ...o ..33
...: .2280 00. 00... 02...... 0:. 005 0.2.... 00... 0:.
r. v n N — ...—5.5.3.5.
.093. 20:80.5»:

 

....EE 22.9865.
he 33:35:80 ”Eb—.3 .53 62508538 Ea.— o..=.m_eE-__uE 3.32:0??— 00 892...... 3.8 ..8 2:3:— oaaavm .28.— 5— 033—.

Unexposed surfaces did have higher a* values than exposed surfaces due to less light
exposure. Yellowness (b*) values for TRTs 1, 2, and 3 were higher than TRT 4 and 5 for
both exposed and unexposed surfaces. Unexposed b* values were higher in yellowness
scores than the exposed ham surface measurements between the ﬁve treatments. As the
storage day increased, b* values also increased for the unexposed ham surface.

Hardness (kg/g sample) values ranged from 0.16 to 0.34 (Table 11). TRTs 2, 4
and 5 were harder than TRT 3. Treatment 3 was the softest in texture. These results are
supported by a study conducted by Hill and Prusa (1988) that documented lean beef
patties treated with 1% MC or HPMC were signiﬁcantly more tender than the control.
DeFreitas and others (1997) noted that the addition of 0.5% KC increased hardness of
cooked pork sausage. Increased hardness values were also documented for structured
beef rolls with 0.5 and 1.0% KC (Shand and others 1994) and beaker pork sausage
manufactured with 0.5% KC (Trius and others 1994). These examples of increased
hardness values are desirable attributes in high-moisture ham products. As the amount of
water is increases in a high-moisture restructured ham there is a loss of textural integrity.
Hydrocolloid gums may give the processor the ability to increase water levels yet
maintain textural quality. Treatment 5 exhibited the highest values for springiness,
cohesiveness, chewiness, and resilience while TRT 3 exhibited the lowest. Mittal and
Barbut (1993) also found that cellulose gums decreased springiness and cohesiveness in
low-fat cooked breakfast sausage. These results indicate that the addition of MC and/or
HPMC may create a softer, looser bound product that is less resilient to external factors.

Kramer shear force (kg/g) values ranged from 0.37 to 0.50 kg/g with TRT 3

requiring the least force to shear throughhe ham slice (Table 11). TRT 4 required the

124

 

.4

Table 1]: Least square means for TPA and 5-blade Kramer shear of high-moisture
restructured ham manufactured with varying combinations of

hydrocolloid brines.

 

 

 

 

 

 

 

 

Hydrocolloid Typed
Treatment‘ 1 2 3 4 5
MC I/KC HPMC l/KC MC I/HPMC I/KC KC Control
Level' 0.4 / 0.6 0.6 / 0.6 0.4 / 0.6 / 0.6 0.6 0.0 SEM“
TPA‘
Hardness
(kg/g sample)h 0.26“h 0.32“ 0.16b 0.34“ 0.34“ 0.02
Springiness
(mm/kg)' 0.88“ 0.86“b 0.78b 0.91“ 0.93“ 0.02
Cohesivenessi 0.59b 0.55““ 0.52“ 0.70“ 0.71“ 0.01
Chewiness (kg)k 0.53bc 0.62““ 0.24c 0.82“b 0.84“ 0.08
Resilience' 0.26b 0.23b 0.19“ 0.35“ 0.36“ 0.01
Kramer Shear'“
Force (kg/g)NS 0.42 0.48 0.37 0.50 0.41 0.04

 

“ Means having different superscripts within rows are signiﬁcantly different (p<0.05).

d Hydrocolloid Type: kappa carrageenan Gelcarin® ME 6910, methylcellulose I:
METHOCELTM A4M, hydroxypropyl methylcellulose I: METHOCELTM F 4M .

°Treatment identiﬁcation for the brine solutions

f Level (0.0, 0.4 & 0.8%) of hydrocolloid type added to brine solution and meat model.

I‘Texture proﬁle analysis: 2- cycle compression using a 5 kg load cell, 75 mm plate and a
heavy duty platform.

i’Hardness is the peak force (kg) during ﬁrst compression / sample weight (kg).

fSpringiness is the height the food recovers between the ﬁrst and second compression.

’ Cohesiveness is the ratio of positive force area during the 2nd compression to that during the
ﬁrst compression (Ag/A1).

1‘ Chewiness is the product of Hardness*Cohesiveness* Springiness.

1 Resilience is the ratio of the area during the l“t plate withdrawal over the 1"t plate penetration.

m Kramer Shear: utilizing 50 kg load cell, S-blade attachment, and heavy duty platform.

” Standard Error of the Mean (SEM).

”5 Not signiﬁcant (P>0.05)

125

most force to shear through the ham slice (0.50 kg/g). These results suggest a trend that
with the addition of MC and HPMC in combination (TRT 3) tenderness increases. The
addition of hydrocolloids to the formulation may be diluting the protein network;
decreasing protein-protein interactions thereby decreasing product bind. Studies
conducted on low-fat beef patties showed lower shear force values for patties that were
manufactured with hydrocolloid gums (Hill and Prusa 1988; Troy and others 1999).
Steinke (2001) also documented lower shear force values for cooked chicken patties
treated with 0.25 and 0.50% MC (2.74-2.96 N) compared to the control (3.94 N). These
studies indicate that the addition of MC and KC (TRT 1) may increase the tenderness of a
ﬁnished product by the creation of protein-hydrocolloid interactions.

Hardness, juiciness, mouth residue/coating and intensity of off ﬂavor were
evaluated by a trained sensory panel (Table 12). Hardness values ranged from 2.2 to 3.3
on an 8-point hedonic scale; with TRTs 4 and 5 being the hardest and TRT 2 the soﬂest
in texture. In general, TRTs 1, 2, and 3 were softer than the TRT 5. Previous sensory
studies noted that the addition of 1.0% HPMC increased tenderness in low-fat ground
beef patties (Hill and Prusa 1988). Additionally, perceived hardness by the sensory panel
and hardness results from texture proﬁle analysis can be correlated. Both textural
analyses, results suggest a trend that with the increase use of hydrocolloid gums (TRT l,
2, and 3) there is a decrease in ﬁrmness.

Juiciness values ranged ﬁom 2.0 to 3.7 with TRT 4 and 5 (3.7 and 3.5) being
evaluated the as the juiciest. In a previous study, panelistsperceive d turkey breasts with
0.5% KC to be juicier than breasts containing starch or the control (Bater and others

1992). Yet, a study conducted on high-moisture hams reported that hams with 1.5%

126

.szmV 582 05 do Sum 2355.
.Uoo -ov N 238388 notes—gm 2:335 :mE \ozEmou ~93: R33. 3088on has: b08055 Hm .

ﬁgmmﬁo 0: $223.. 0: >06 30805on8 32:02:81
”2an £53: “Eon w cm :0 comma 3:553 33255 322 “a 363:8 Baum hem—How BEE... 2
dado:— 32: Ba cows—om 2:5 3 non—ca 25 223863 «o ded a. vd ddv .025 m
28:28 2:5 mo 22285202 2258.:

.2: 52200582 2 82232282 E22256:

.23. 5280252 2 822322.88 .22. m: @2830 2.28228 8&2 825 22382;: .
Amodvnd Eobbd 338$:me 2a 958 £525 Emcomuoaam “couobmd wEZE .2802 3

 

 

 

 

 

_ d no; no; ta.— ﬁN._ .1.— Hog—”Tho
mo big—85
Nd BdN cm; L .v ﬁnd ndN was—woo 32.23% 5:02
Nd and Ram pdN nvN ncN 30533.
Nd ﬁdd «mgr. BVN oN.N SYN 32.6.83
amouaatuxx

_me dd dd 0d \ dd \ wd 0d \ ed 0d \ vd "—261—

 

 

 

.8250 Dv— Uvs USED 02 UV:— UEL—m 0v!— DE

 

 

m w m N 2 2.5.58;

 

.22.? 22.82%:

 

.85.:— Ee=ooEFE he 3035:5259 an???» :33 coaaoauznaﬁ
Ea.— coasuosuumoa 2:33.215:— ue 8:52.? fem—.3. 62:95 ..8 2:3:— oaaag 3.3..— ”NH 035,—.

127

carrageenan received lower juiciness scores than those without carrageenan (Prabhu and
Sebranek 1997). The decrease in perceived juiciness scores seen by Prabhu and Sebranek
(1997) may be due to high amounts of KC (1.5%) added. When comparing juiciness
between treatments, ham slices containing MC and/or HPMC (TRT l, 2, and 3) scored
signiﬁcantly lower in juiciness values. These results contradict Hill and Prusa (1988)
who observed an increase in juiciness with the addition of 1.0% HPMC and MC in low-
fat beef patties. Additionally, Steinke (2001) utilizing 0.25 and 0.50% MC in chicken
patties stated that the addition of MC increased perceived juiciness. Furthermore, Mittal
and Barbut (1993) reported that the addition of carboxymethyl and microcrystalline
cellulose at 1.0% did not effect juiciness perception by a sensory panel. Difference in
these results from previous studies may be due to the combination of MC and/or HPMC
with KC.
Mouth coating/residue values ranged from 1.5 to 4.1 on an 8-point hedonic scale
(Table 12). Treatment 3 had the highest (4.1) perceived mouth residue/coating with TRT
2 (3.7) being similar in mouth-residue to TRT 3. These results were expected as MC
and/or HPMC can form a slick coating on surfaces. For example, HPMC has been used
as a surface barrier in ﬁ'ied foods. French ﬁ'ies dipped in HPMC prior to frying resulted
in less greasy French ﬁies (Grover 1986). Additionally, ﬁied Boondis manufactured with
1.0 % HPMC decreased oil content by 22.7% when compared to the control (Priya and
others 1996).
No off-ﬂavors were detected by TRTs 4 and 5 by the trained sensory panel
(Table 12). Treatment 3 was perceived to have the most off-ﬂavor (1.4) between the

treatments. The addition of 1.0% HPMC to low-fat beef patties signiﬁcantly increased

128

the intensity of off-ﬂavor when compared to the control (Hill and Prusa 1988). Off-
ﬂavor intensity and residue/mouth coating may be the biggest draw backs of using MC
and HPMC in combination as it may severely hinder consumer acceptability.
Conclusions

The results of this study indicate that the addition of MC and/or HPMC with KC
can control purge in restructured high-moisture ham. Speciﬁcally, TRT 1 demonstrated
high cook yield values and decreased purge values when compared to TRT 4 and 5.
Additionally, TRT 1 had a positive effect upon color (L*, a*, b*) values and stability.
Lightness values of TRTs 1, 2, and 3 were decreased and held over a 28 day storage
period when compared to TRT 4 and 5. Texture proﬁle analysis and Kramer shear values
also indicated that TRT 3 was more tender requiring less force to shear. Increased
mechanical tenderization results were conﬁrmed by the trained sensory panel. The
addition of MC I with KC (TRT 1) has demonstrated to it maybe a valuable purge
controller. However, the use of MC and/or HPMC does have a potential set back.
Trained sensory panelists have detected an off-ﬂavor associated with MC and HPMC.
This is supported by previous a study conducted by Hill and Prusa (1988) utilizing 1%
MC and HPMC. Based on these results, TRT 1 should be studied further due its purge
controlling and quality assuring abilities. Future research should be directed towards the
masking of MC’s off-ﬂavor to make this application more appealing to the meat

processor and consumer.

129

References

AMSA. 1995. Research guidelines for cookery, sensory evaluation, and instrumental
measurements of fresh meat. American Meat Science Association and National Livestock
and Meat Board. Chicago, IL.

AOAC. 2000. Meat and meat products. In: Cunniff, P, editor. Ofﬁcial methods of
analysis of AOAC International. Washington DC: AOAC International. P 1-23.

Barbut, S, Maurer, AJ, Lindsay, RC. 1988. Effects of reduced sodium chloride and
added phosphates on physical and sensory properties of turkey frankfurters. J Food Sci
53(1):62-66.

Bater, B, Descamps, O, Maurer, AJ. 1992. Quality characteristics of hydrocolloid added
oven roasted turkey breasts. J Food Sci 57(7): 1068-1070.

Bater, B, Descamps, O, Maurer, AJ. 1993. Quality characteristics of cured turkey thigh
meat with added hydrocolloids. J Poult Sci 72:349-354.

DeFreitas, Z, Sebranek, JG, Olson, DG, Carr, J M. 1997. F reeze/thaw stability of cooked
pork sausage as affected by salt, phosphate, pH, and carrageenan. J Food Sci 62(3):551-
554.

Grover, JA. 1986. Food Hydrocolloids, Vol III. Glicksman, M, editor. Boca Raton, FL:
CRC Press Inc. P 121-154.

F oegeding, EA, Ramsey, SR. 1986. Effect of gums on low-fat meat batters. J Food Sci
51:33-35, 46.

Hill, SE, Prusa, KJ. 1988. Physical and sensory properties of lean ground beef patties
containing methylcellulose and hydroxypropyl methylcellulose. J Food Qua] 11:331-
337.

Keeton, JT, Foegeding, EA, Patana-Anake, C. 1984. A comparison of non-meat proteins,
sodium tripolyphosphate and processing temperature effects on physical and sensory
properties of frankfurters. J Food Sci 49: 1462-1465.

Matlock, RG, Terrell, RN, Savell, JW, Rhee, KS, Dutson, TR. 1984. Factors affecting
properties of precooked-frozen pork sausage patties made with various NaCl/phosphate
combinations. J Food Sci 49:1372-1375.

Meilgaard, M, Civille, GV, Carr, ET. 1991. Sensory Evaluation Techniques, Boca Raton,
FL: CRC Press Inc.

Mittal, GS, Barbut, S. 1993. Effects of various cellulose gums on the quality parameters
of low-fat breakfast sausages. Meat Sci 35:93-103.

130

Prabhu, GA, Sebranek, JG. 1997. Quality characteristics of ham formulated with
modiﬁed corn strarch and kappa carrageenan. J Food Sci 62(1):198-202.

Priya, R, Singhal, RS, Kulkami, PR. 1996. Carboxymethylcellulose and hydroxypropyl
methylcellulose as additives in reduction of oil content in batter based deep-fat fried
boondis. Carb Poly 29:333-335.

Rhee, KS. 1978. Minimization of further lipid peroxidation in the distillation 2-
thiobarbutiric acid test of ﬁsh and meat. J Food Sci 43:1776-1778.

SAS Institute, Inc. 2002. SAS user’s guide, version 8.2. Cary, NC: SAS Institute.

Schwartz, WC, Mandigo, RW. 1976. Effect of salt, sodium tripolyphosphate, and storage
on restructured pork. J Food Sci 41 : 1266-1269.

Shand, PJ, Sofos, JN, Schmidt, GR. 1993. Properties of algin/calcium and salt/phosphate
structured beef rolls with added gums. J Food Sci 58(6):]224-1230.

Shand, PJ, Sofos, JN, and Schmidt, GR. 1994. Kappa-carrageenan, sodium chloride and
temperature affect yield and texture of structured beef rolls. J Food Sci 59(2):282-287.

Steinke, LW. 2001. Moisture management and texture enhancement in chicken patties
containing methylcellulose [MS thesis] East Lansing, MI: Michigan State University. 123
p. Available from: Michigan State University.

Tarladigis, GG, Wats, BM, Younthan, MT, Dugan, L Jr. 1960. J Am Oil Chem 37:44-48.

Trius, A, Sebranek, JG, Rust, RE, Carr, JM. 1994 B. Carrageenans in beaker sausage as
affected by pH and sodium tripolyphosphate. J Food Sci 59(5):946-951.

Troy, DJ, Desmond, EM, Buckley, DJ. 1999. Eating quality of low-fat beef burgers
containing fat-replacing functional blends. J Sci Food Agric 79:507-516.

USDA. 2002. Food Safety and Inspection Service (F SIS). hum//www.fsis.usda.gov/.

Zipser, MW, Wast, BM. 1962. Lipid oxidation. Food Technol 16(7):102.

131

APPENDICES

132

APPENDIX 1: Experiment 1 Water Solution Formulation and Procedures

 

Solution Formulations:

 

 

 

 

 

 

 

 

 

 

Hydrocolloid Hot water lce+ chilled water Total wt.
Treatment (g) (g) (gL (g)
0.2% MC or HPMC 1.82 302.39 604.79 909.00
0.4% MC or HPMC 3.64 301.79 603.57 909.00
0.6% MC or HPMC 5.45 301.18 602.37 909.00
0.8% MC or HPMC 7.27 300.58 601.15 909.00
0.2% KC 1.82 0.00 907.18 909.00
0.4% KC 3.64 0.00 905.36 909.00
0.6% KC 5.45 0.00 903.55 909.00
0.8% KC 7.27 0.00 901.73 909.00

 

 

 

 

 

 

MC or HPMC Brine Manufacture:

1.

6.

Add appropriate amount of hot water (85°C) according to treatment ﬁ'om above table
to 946.4 mL glass jar.

Add MC (A4M) or HPMC (F4M, K4M) (The Dow Chemical Company, Midland,
MI).

Mix with 4-blade mixing head: 2-blades perpendicular (2.54 cm across) to shaft and 2
blades parallel to shaﬁ (1.27 cm equidistant from shaft) attached to a drill (SKIL, S-B
Power Tool Co., Chicago, IL). Mix for 5 minutes until MC or HPMC is well blended

(begin timing once all is added).

Add 1/2 and 1/2 water and ice mixture (< 4.4°C) slowly to dispersed MC or HPMC
solution. Mix for 10 minutes (begin timing once all water is added).

Repeat steps for each MC/HPMC marinade (n=12).

KC Solution Manufacture:

1. Add appropriate amount of chilled water (< 4.4°C) according to treatment from above

table to 946.4 mL glass jar.

Add KC (Gelcarin ME 6910, FMC BioPolymer, Princeton, NJ) and mix for 10
minutes (begin timing once all KC is added).

Mix with 4-blade mixing head: 2-blades perpendicular (2.54 cm acrosslo shaft and 2

blades parallel to shaft (1 .27 cm equidistant from shaft) attached to a drill (SKIL, S-B
Power Tool Co., Chicago, IL). Mix for 5 minutes until MC or HPMC is well blended
(begin timing once all is added).

4. Repeat steps for each KC marinade (nﬂ)

133

APPENDIX 2: Experiment H and III Brine Solution Formulations and Procedures

 

Brine Formulations:

 

 

 

 

 

 

 

45% Addition 0.20 %
lbs g 45% ppm
Water 1.89 858.06
Salt 0.0803 36.46 1.80
Nitrite 0.000784 0.36 156.18 ('156)
Sugar 0.0119 5.40 0.27
Erythorbate 0.001263 0.57 251.76 ('550)
Phosphate 0.0135 6.13 0.30
MC/HPMC/KC 0.0089 4.04 0.200
Total 2.006647 911.0175
45% Addition 0.40 %
lbs g 45% ppm
Water 1.88 853.52
Salt 0.08 36.32 1.80
Nitrite 0.000783 0.36 156.18 ('156)
Sugar 0.012 5.45 0.27
Erythorbate 0.001262 0.57 251.72 ('550)
Phosphate 0.0135 6.13 0.30
MC/HPMC/KC 0.01784 8.10 0.400
Total 2.005385 910.4448
45% Addition 0.60 %
lbs g 45% ppm
Water 1.87 848.98
Salt 0.08 36.32 1.80
Nitrite 0.000783 0.36 156.17 ('156)
Sugar 0.012 5.45 0.27
Erythorbate 0.001262 0.57 251.86 ('550)
Phosphate 0.0135 6.13 0.30
MC/HPMC/KC 0.02674 12. 14 0.600
Total 2.004285 909.9452

 

 

134

 

 

 

 

45% Addition

 

lbs g
Water 1 .86 844.44
Salt 0.08 36.32
Nitrite 0.000782 0.36
Sugar 0.012 5.45
Erythorbate 0.001261 0.57
Phosphate 0.0135 6.13
MC/HPMC/KC 0.0356 16.16
Total 2.003143 909.4269

0.80%

45% ppm
1.80

156.15 ('156)
0.27

251.80 ('550)
0.30
0.800

 

MC or HPMC Brine Manufacture:

1. Add appropriate amount of chilled water (< 4.4°C) according to treatment from above

table to 946.4 mL glass jar.

2. Add Briﬁsol 512 sodium phosphate (BK Giulini Corporation, Simi Valley, CA).

3. Mix with 4-blade mixing head: 2-blades perpendicular (2.54 cm across) to shaﬁ and 2
blades parallel to shaﬁ (1.27 cm equidistant from shaﬁ) attached to a drill (SKIL, S-B
Power Tool Co., Chicago, IL). Mix for 5 minutes until MC or HPMC is well blended

(begin timing once all phosphate is added).

4. During phosphate mixing time, place MC (A4M) or HPMC (F 4M, K4M) (The Dow
Chemical Company, Midland, MI) in a beaker with the salt and sugar. Mix well by
hand to fully disperse MC or HPMC.

(It

F"

KC Brine Manufacture:

1. Add appropriate amount of chilled water (< 4.4°C) according to treatment from above

table to 946.4 mL glass jar.

2. Add Briﬁsol 512 sodium phosphate (BK Giulini Corporation, Simi Valley, CA).

3. Mix with 4-blade mixing head: 2-blades perpendicular (2.54 cm across) to shaft and 2
blades parallel to shaft (1.27 cm equidistant ﬁom shaft) attached to a drill (SKIL, S-B

. Add MC or HPMC mixture and mix with drill mixer for 10 minutes (begin timing
mixing once all mixture is fully added).

Repeat steps for each MC/HPMC marinade (n=12).

135

 

Power Tool Co., Chicago, IL). Mix for 5 minutes until MC or HPMC is well blended
(begin timing once all phosphate is added).

Add salt and mix for 2 minutes (begin timing once all of salt is added).

Add KC (Gelcarin ME 6910, F MC BioPolymer, Princeton, NJ) and mix for 3 more
minutes (begin timing once all KC is fully added).

Add sugar and mix for 2 more minutes (begin timing once all sugar is added).

Repeat steps for each KC marinade (n=4).

Nitrite and Erythorbate Addition:

1.

2.

12-16 hours aﬁer initial brine manufacturing.
Mix with 4-blade mixing head: 2-blades perpendicular (2.54 cm across) to shaft and
2 blades parallel to shaft (1.27 cm equidistant from shaft) attached to a drill (SKIL, S-

B Power Tool Co., Chicago, IL). Mix for 5 minutes until MC or HPMC is well
blended (begin timing once all is added).

Add sodium nitrite (J .T. Baker, Phillipsburg, NJ) then sodium erythorbate (Butcher
and Packer Supply Co., Detroit, MI) and mix for an additional minute.

Repeat for each treatment (n=16)

136

APPENDIX 3: Experiment IV Brine Formulations and Procedures

 

Brine Formulations:

 

 

 

 

 

 

 

 

45% Addition Control
lbs g 45% ppm
Water 1 .9 862.60
Salt 0.0803 36.46 1.80
Nitrite 0.000784 0.36 156.19 ('156)
Sugar 0.0119 5.40 0.27
Erythorbate 0.001263 0.57 251.63 ('550)
Phosphate 0.0135 6.13 0.30
Total 2.007747 911.5171
45% Addition MC I 0.4% / HPMC I 0.6 %
lbs g 45% ppm
Water 1.85 839.90
Salt 0.08 36.32 1.80
Nitrite 0.000782 0.35 156.14 ('156)
Sugar 0.012 5.45 0.27
Erythorbate 0.001261 0.57 251.84 ('550)
Phosphate 0.0135 6.13 0.30
MC I 0.01781 8.09 0.400
HPMC 1 0.0267 12.12 0.600
Total 2.002052 908.9316
45% Addition MC I 0.4% / KC 0.6%
lbs g 45% ppm
Water 1.85 839.90
Salt 0.08 36.32 1.80
Nitrite 0.000782 0.35 156.14 ('156)
Sugar 0.012 5.45 0.27
Erythorbate 0.001261 0.57 251.84 ('550)
Phosphate 0.0135 6.13 0.30
MC I 0.01781 8.09 0.400
KC 0.0267 12.12 0.600
Total 2.002052 908.9316

 

1.37

 

 

 

 

 

 

 

 

 

45% Addition HPMC I 0.6% / KC 0.6%
lbs g 45% ppm
Water 1.84 835.36
Salt 0.08 36.32 1.80
Nitrite 0.000781 0.35 156.15 ('156)
Sugar 0.012 5.45 0.27
Erythorbate 0.00126 0.57 251.88 ('550)
Phosphate 0.0135 6.13 0.30
HPMC 1 0.0267 12.12 0.600
KC 0.0267 12.12 0.600
Total 2.000941 908.4273
45% Addition MC I 0.4%/HPMC I 0.6%/KC 0.6%
lbs g 45% ppm
Water 1.825 828.55
Salt 0.08 36.32 1.80
Nitrite 0.000782 0.36 156.13 ('156)
Sugar 0.012 5.45 0.27
Erythorbate 0.001262 0.57 251.85 ('550)
Phosphate 0.0135 6.13 0.30
MC I 0.01781 8.09 0.400
HPMC I 0.0267 12.12 0.600
KC 0.0267 12.12 0.600
Total 2.003754 909.70

 

 

 

MC and HPMC combination Brine Manufacture:

1. Add appropriate amount of chilled water (< 4.4°C) according to treatment ﬁ'om above
table to 946.4 mL glass jar.

2. Add Briﬁsol 512 sodium phosphate (BK Giulini Corporation, Simi Valley, CA).

3. Mix with 4-blade mixing head: 2-blades perpendicular (2.54 cm across) to shaft and 2
blades parallel to shaft (1.27 cm equidistant from shaft) attached to a drill (SKIL, S-B
Power Tool Co., Chicago, IL). Mix for 5 minutes until MC or HPMC is well blended
(begin timing once all phosphate is added).

4. During phosphate mixing time, place MC 1 (A4M)and HPMC I (F4M) (The Dow
Chemical Company, Midland, MI) in a beaker with the salt and sugar. Mix well by
hand to fully disperse MC and HPMC.

138

5. Add MC I and I-IPMC I mixture. mix with drill mixer for 10 minutes (begin timing
mixing once all mixture is fully added).

6. Repeat steps for each MC and HPMC brine (n=1).

KC with MC I and/or HPMC I Brine Manufacture:

1. Add appropriate amount of chilled water (< 4.4°C) according to treatment from above
table to 946.4 mL glass jar.

2. Add Briﬁsol 512 sodium phosphate (BK Giulini Corporation, Simi Valley, CA).

3. Mix with 4-blade mixing head: 2-blades perpendicular (2.54 cm across) to shaft and 2
blades parallel to shaft (1 .27 cm equidistant from shaft) attached to a drill (SKIL, S-B
Power Tool Co., Chicago, IL). Mix for 5 minutes until MC or HPMC is well blended
(begin timing once all phosphate is added).

4. Add salt and mix for 2 minutes (begin timing once all of salt is added).

5. During phosphate mixing time, place MC I (A4M) and/or HPMC I (F4M) (The Dow
Chemical Company, Midland, MI), KC (Gelcarin ME 6910, FMC BioPolymer,
Princeton. NJ) and sugar in beaker, mix thoroughly by hand.

6. Add MC and/or HPMC and KC mixture, mix with drill mixer for 10 minutes (begin
timing mixing once all mixture is fully added).

7. Repeat steps for each combination brine (n=3).

Control Brine Manufacturing:

1. Add appropriate amount of chilled water (< 4.4°C) according to treatment from above
table to 946.4 mL glass jar.

2. Add Briﬁsol 512 sodium phosphate (BK Giulini Corporation, Simi Valley, CA).

3. Mix with 4-blade mixing head: 2-blades perpendicular (2.54 cm across) to shaft and 2
blades parallel to shaft (1 .27 cm equidistant from shaft) attached to a drill (SKIL, S-B
Power Tool Co., Chicago, IL). Mix for 5 minutes until MC or HPMC is well blended
(begin timing once all phosphate is added).

4. Add salt and mix for 2 minutes (begin timing once all of salt is added).

5. Add sugar and mix for 2 more minutes (begin timing once all sugar is added).

139

 

7.

Repeat steps for each control brine (n=1).

Nitrite and Erythorbate Addition:

1.

Ex)

12-16 hours after initial brine manufacturing.

Mix with 4-blade mixing head: 2—blades perpendicular (2.54 cm across) to shaft and
2 blades parallel to shaft (1.27 cm equidistant from shaft) attached to a drill (SKIL, S-
B Power Tool Co., Chicago, IL). Mix for 5 minutes until MC or HPMC is well
blended (begin timing once all is added).

Add sodium nitrite (J .T. Baker, Phillipsburg, NJ) then sodium erythorbate (Butcher
and Packer Supply Co., Detroit, MI) and mix for an additional minute.

Repeat for each treatment (n=5)

140

APPENDIX 4: Programmed Water Bath Procedure

 

Water Bath Procedure:

1.

PolyScience programmable water bath was turned on and program was initiated
30 minutes before sample entry; allowing water bath to achieve 40°C to simulate
temperature of actual samples.

Hydrocolloid water solution, brine solution or meat samples were then placed into
water bath at 4°C, thermally processed ﬁom stages 2-6, and cooled in stage 7 to
simulate the shower cycle.

Remove samples from water bath and analyze as necessary.

This processes was repeated three times for each repetition as only 18 samples
(n=6) could be thermally processed at one time.

Programming PolyScience Circulator with Digital Controller Bath:

(Model 9510, PolyScience, Niles, IL)

To begin entering program, press FCN then #5. Select what program
number you want to name the program ( l or 2).

Upon number selection you will see the word transferring. Select #1= display,
edit and write a program. This will then allow you to enter temperatures and time

points. Press enter after each item.

Up to 10 temperature/time steps can and must be entered. Repeat last step until
you reach step 10.

After passing all 10 steps enter number of cycles you wish the water bath
to go through (1-999 times).

At end of program select soak or power off when done. Selecting soak allows for
water bath to hold at ﬁnal constant temperature entered indeﬁnitely.

Select #1 or 2 to store your new program.

Water bath is now programmed and ready to conduct process.

141

APPENDIX 5: Viscometer Calibration and Viscosity Determination

 

Calibration Procedure:

1.

Turn power on to Brookﬁeld Viscometer (Model DV-II, Brookﬁeld Engineering

laboratories, Stoughton, MA). Set speed dial to 12, and turn motor on.
Press auto zero. Display will start blinking.

When blinking stops turn motor off. Do not turn off power switch.

Press SPDL then enter spindle number (01 . . .07). Example: spindle 3 = 03.
Press desired unit button (%, cPs, SS). Centipoise (cPs) was used.

Viscometer is now calibrated.

Viscosity Reading Procedure:

1.

Place selected spindle slowly into brine/solution at a 45° angle. Look for air
bubbles under spindle. If air bubbles are present, remove spindle and try again.

Attach spindle to viscometer, not allowing spindle to come out of sample.

Adjust spindle height. Solution should be level with notched ring around spindle
neck.

Turn motor on.
Allow reading to equilibrate and record measurement.

Turn off motor, but do not turn off power to viscometer. If power is shut off re-
calibrate viscometer.

Detach spindle, clean with distilled water, and dry with paper towel.

Repeat as necessary.

142

APPENDIX 6:

TA—HDi Gel Strength Settings

 

Texture Analyzer:

TA-HDi Settings:
Mode:

Option:

Pre-Test Speed:

Test Speed:

Post-Test Speed:
Pre-Travel Distance:
Compression Distance:
Trigger Type:

Data Acquisition Rate:

Attachment/Accessory:

TA-HDi Texture Analyzer
Texture Technologies Corporation, Scarsdale, NY

Measure Force in Compression
Return to Start

5.0 mm/s

0.20 mm/s

10 mm/s

51.0 mm/s

8 mm

Return

200 pps

-TA-10; 12.7mm AOAC acrylic cylinder, 35mm tall
-5 kg load cell
-TA-90; Heavy duty platform

143

APPENDIX 7:

2-Cycle Compression Settings for Meat Model

 

Texture Analyzer:

TA-HDi Settings:
Test Mode:

Option:

Pre-Test Speed:
Test Speed:
Post-Test Speed:
Pre-Travel Distance:

Compression Distance:

% Compression:
Trigger Type:

Data Acquisition Rate:

Attachment/Accessory:

TA-HDi Texture Analyzer
Texture Technologies Corporation, Scarsdale, NY

TPA

Return to Start

2.00 mm/s

1.67 mm/s

1.67 mm/s

24.5 mm

sample size x 0.25

Compressed to 25% of original height (75% compression)
Return

200 pps

-TA-30: 75mm aluminum plate, 10mm tall
-5 kg load cell
-TA-90; Heavy duty platform

144

APPENDIX 8: Proximate Composition

 

AOAC. 2000. Meat and meat products. In P. Cunniff (Ed.), Ofﬁcial methods of analysis
of AOAC International. 1-23p. Washington, DC: AOAC International.

Sample Preparation (modiﬁed from section 983.18 Meat and Meat Products)

1.

Section meat into very small (<1 cm squares) pieces. If already frozen, smash
samples with a hammer to decrease size of sample for ease of grinding.

Add sample to Tekmar grinders (Tekmar Co, Cincinnati, OH) ﬁlling grinding
chamber half full.

Then add dry ice to ﬁll up chamber.

Grind 2 to 3 minutes using Tekmar grinder (Tekmar Co, Cincinnati, OH) until sample
is ground into a ﬁne powder. It may be necessary to stop in the middle of grinding
and stir the sample up for uniform grinding.

Transfer ﬁnely ground powder to labeled whirl pack bags. Loosely close bag so that
dry ice can evaporate and dissipate. This takes about 2 days. Place in ﬁeezer
immediately to prevent melting of powder.

Moisture Analysis

6.

Place a medium weigh boat on scale and zero. This is to keep the scale clean. Add
paper labeled with sample ID and paperclip. Record the weight then tare the scale.

Add 2 grams (3: .03 g) of thoroughly mixed sample to the paper. Once desired weight
is reached record weight and fold over top. Secure by folding and tucking top. Place
flat on tray. Do all samples in triplicate. Do not stack samples on tray. This will
hinder the drying process.

Once tray is full, place in drying oven set at 100°C for 20 - 24 hours.

After drying, place samples using latex gloves or tongs in dessicator to cool
completely before weighing. Once cool, weigh samples and record. This is your ﬁnal
weight for moisture and your initial weight for fat analysis. Use the following formula

to determine the percent moisture in your samples:

Moisture (%)= wet mph wt. — dry sample wt. x 100
wet sample wt.

145

Fat Analysis Using Soxhlet Ether Extraction

 

10. Take samples from moisture analysis and place in extraction tubes. Make sure that
all the samples are below the level where the ether drains off (curved glass on
outside of tube).

1]. Add petroleum ether to clean boiling ﬂasks until about 5% full. Add 2 to 3 glass beads
as a boiling aid.

12. Connect the extraction ﬂask to the boiling ﬂask and Soxhlet apparatus. Place
paraﬁhn on the joint. Mount both to the condensing units on top of extraction ﬂasks
using paraﬁlm around joint.

13. Turn on condensing water so it runs at a steady stream.

14. Set Rheostats on high and run for 24 hours.

15. Place ether soaked samples onto a tray in a hood for 2 hours to allow ether to
dissipate.

16. Place samples in drying oven for 5 to 10 min to remove any possible moisture then
place in dessicator for 1/2 hour to cool.

17. Weigh and record the weight of the samples. Calculate fat on wet basis with the
following equation:

Fat (%) = dry sample wt. — extracted sggle wt. x 100
wet sample wt.
Protein Analysis
1. Weigh out approximately 1 gram of powdered meat into the tared crucible. Write the

weight and sample ID on the side of the crucible with pencil.

After weighing out samples, dry for 18 to 20 hours in the drying oven at 100°C. This
removes moisture that can cause internal malfunctions with the Leco Protein
Analyzer. Do not reweigh samples. Enter wet weight into computer.

ProcedlLes for the LECO PP 2000 Nitrogen Analyzer

1.

Open valves completely on oxygen, helium and compressed air tanks. Make sure

tanks have adequate levels of gas (gauge should read >100psi) and that the pressure

out of the tanks are set at 40 psi.

146

. Press escape on upper left hand corner of touch screen until “front panel” comes up
and then press it. On right hand side of screen a section labeled “analysis gas” can be
found. Push the “on” button to turn gasses on to the machine. Check to see that your
furnace temperature is 1050°F (located on left part of screen).

. Wait about 5 minutes for all gasses to equilibrate then start your leak tests. Press
escape from the front panel located in upper left corner. A screen with several icons
will appear. Press “maintenance”. This will bring up helium leak test, combustion
leak test and ballast leak test icons. Press the helium leak test. If it passes move onto
the combustion leak test. Once ﬁnished, start running blanks. Run a ballast test as it is
part of the combustion system.

. Run several air blanks through to purge the system. To do this escape from the
“maintenance” section and push the “analyze” icon. On the bottom of the screen you
will see several commands. Push “select [D code”. Toggle the highlighted line using
the arrows to blanks. Then push exit on bottom. Then push manual weight. This will
bring up a touch screen with 0.2000000 on it. Push the enter button at least 10 times
to bring up 10 rows of 0.20000. Then push analyze. The machine will run through
these ten samples. Numbers should come down to about <.030% protein.

. Once blanks are at an acceptable number, run 4 to 5 EDTA samples (approximately
0.5g) to verify machine is operating properly.

. Weigh EDTA samples out in the ceramic boats and write the weight on the side in
pencil (at least three decimal places).

. Select “manual weight” and put your weight into the machine pushing enter after
each entry. Once weights are entered, push analyze. Follow the directions on the
touch screen. Push your ﬁrst sample into the chamber about one half inch so the door
doesn’t catch the boat. Push okay on the screen when it asks you place your sample in
the chamber. The next message will tell you to wait because the system is purging.
Then the machine will then tell you to push the boat into the chamber. The machine
will combust and analyze the sample in approximately 3 minutes.

. Analyze samples as described in step 7.

147

APPENDIX 9: Study II Brine Formulation and Procedures

 

Brine Formulations:

 

 

 

 

 

 

 

45% Addition MC I 0.4% / KC 0.6%
lbs g 45% ppm
Water 23.1 10487.40
Salt 1.0 454.00 1.80
Nitrite 0.009758 4.43 156.15 ('156)
Sugar 0.15 68.10 0.27
Erythorbate 0.01572 7.14 251.56 ('550)
Phosphate 0.165 74.91 0.30
MC I 0.2223 100.92 0.400
KC 0.333 151.18 0.600
Total 24.99578 1 1348.08
45% Addition HPMC 0.6% / KC 0.6%
lbs g 45% ppm
Water 23 10442.00
Salt 0.999 453.55 1.80
Nitrite 0.009763 4.43 156.17 ('156)
Sugar 0.15 68.10 0.27
Erythorbate 0.015726 7.14 251.56 ('550)
Phosphate 0.165 74.91 0.30
HPMC I 0.3332 151.27 0.600
KC 0.3332 151.27 0.600
Total 25.00589 11352.67
45% Addition MC I 0.4%/HPMC I 0.6%/KC 0.6%
lbs g 45% ppm
Water 23 10442.00
Salt 1.01 458.54 1.80
Nitrite 0.009858 4.48 156.15 ('156)
Sugar 0.15 68.10 0.27
Erythorbate 0.015882 7.21 251.56 ('550)
Phosphate 0.17 77.18 0.30
MC I 0.2245 101.92 0.400
HPMC I 0.3365 152.77 0.600
KC 0.3365 152.77 0.600
Total 25.25324 11464.97

 

148

 

 

 

 

 

 

 

45% Addition Control
lbs g 45% ppm
Water 24 10896.00
Salt 1.015 460.81 1.80
Nitrite 0.0099 4.49 156.15 ('156)
Sugar 0.15 68.10 0.27
Erythorbate 0.01595 7.24 251.57 ('550)
Phosphate 0.17 77.18 0.30
Total 25.36085 11513.83
45% Addition KC 0.6%
lbs g 45% ppm
Water 23.5 10669.00
Salt 1.005 456.27 1.80
Nitrite 0.009833 4.46 156.16 (’156)
Sugar 0.15 68.10 0.27
Erythorbate 0.01584 7.19 251.56 ('550)
Phosphate 0.17 77.18 0.30
KC 0.336 152.54 0.600
Total 25.18667 11434.75

 

 

KC with MC and/or HPMC Brine Manufacture:

1.

Add appropriate amount of chilled water (< 4.4°C) according to treatment from above
table to white plastic bucket.

Add Briﬁsol 512 sodium phosphate (BK Giulini Corporation, Simi Valley, CA).

Mix with Rotostat mixer (Model 80XP63SS, Admix Inc., Londonderry, NH)
modiﬁed by MSU at 1200 rpm for 2 minutes until phosphate is dissolved (begin
timing once all phosphate is added).

Add salt and mix for 2 minutes with Rotostat mixer (Model 80XP63 SS, Admix Inc.,
Londonderry, NH) modiﬁed by MSU at 1200 rpm (begin timing once all of salt is
added).

During phosphate mixing time, place MC I (A4M) and/or HPMC I (F 4M) (The Dow
Chemical Company, Midland, MI), KC (Gelcarin ME 6910, FMC BioPolymer,
Princeton, NJ) and sugar in beaker, mix thoroughly by hand. .

Add MC I and/or HPMC l and KC mixture, mix with Rotostat mixer (Model
80XP63SS, Admix Inc., Londonderry, NH) modiﬁed by MSU at 1500 rpm for 10
minutes (begin timing mixing once all mixture is fully added).

149

7. Repeat steps for each KC with MC or HPMC combination brine (n=4).

Control Brine Manufacturing:

1. Add appropriate amount of chilled water (< 4.4°C) according to treatment from above

table to plastic bucket.

. Add Briﬁsol 512 sodium phosphate (BK Giulini Corporation, Simi Valley, CA).

Mix with Rotostat mixer (Model 80XP63SS, Admix Inc., Londonderry, NH)
modiﬁed by MSU at 1200 rpm for 2 minutes until phosphate is dissolved (begin
timing once all phosphate is added).

Add salt and mix for 2 minutes with Rotostat mixer (Model 80XP63SS, Admix Inc.,
Londonderry, NH) modiﬁed by MSU at 1200 rpm (begin timing once all of salt is
added)

Add sugar and mix for 2 more minutes with Rotostat mixer (Model 80XP63 SS,
Admix Inc., Londonderry, NH) modiﬁed by MSU at 1200 rpm (begin timing once all
sugar is added).

Repeat steps for each control brine (n=1).

KC Brine Manufacturing:

1.

Add appropriate amount of chilled water (< 4.4°C) according to treatment from above
table to plastic bucket.

Add Briﬁsol 512 sodium phosphate (BK Giulini Corporation, Simi Valley, CA).

Mix with Rotostat mixer (Model 80XP63SS, Admix Inc., Londonderry, NH)
modiﬁed by MSU at 1200 rpm for 2 minutes until phosphate is dissolved (begin
timing once all phosphate is added).

Add salt and mix for 2 nrinutes with Rotostat mixer (Model 80XP63SS, Admix Inc.,
Londonderry, NH) modiﬁed by MSU at 1200 rpm (begin timing once all of salt is
added).

. Add KC (Gelcarin ME 6910, F MC BioPolymer, Princeton, NJ) and mix for 3 more

minutes with Rotostat mixer (Model 80XP63SS, Admix Inc., Londonderry, NH)
modiﬁed by MSU at 1200 rpm (begin timing once all KC is fully added).

150

6. Add sugar and mix for 2 more minutes with Rotostat mixer (Model 80XP63SS,
Admix Inc., Londonderry, NH) modiﬁed by MSU at 1200 rpm (begin timing once all
sugar is added).

7. Repeat steps for each KC brine (n=1).

Nitrite and Erythorbate Addition:
1. 12-16 hours after initial brine manufacturing.

2. Mix brine for 1 minute using Rotostat mixer (Model 80XP63 SS, Admix Inc.,
Londonderry, NH) modiﬁed by MSU at 1200 rpm.

3. Add sodium nitrite (J .T. Baker, Phillipsburg, NJ) then sodium erythorbate (Butcher
and Packer Supply Co., Detroit, MI) and mix for 1 additional minute with Rotostat
mixer (Model 80XP63 SS, Admix Inc., Londondery, NH) modiﬁed by MSU at 1200

rpm.

4. Repeat for each treatment (n=5)

151

APPENDIX 10: Storage Lighting Determination and Conversion Procedure

 

Procedure:

1. Measure size of sliced restructured ham storage cooler. Cooler length and width
were measured 18.583 ft x 16.417 ft (566.41 cm x 500.39 cm).

2. Measure amount of light being emitted by lighting in Foot Candles (FC). A Triple
Range Light Meter (Model 217, General Electric Lighting, Cleveland, OH) was
used to determine Foot Candle reading. FC=80

3. Lumen conversion equation is shown below:

Luminous Flux (Lumen) Conversion:
Square feet = 18.583ft x 16.417 ft = 305.083 sq. feet
1 PC = 1 lumen

sq. foot

80 FC= “x” lumens
305.083 square ft.

 

X= 24, 407 Lumens

152

APPENDIX 11: Cook Yield Determination

 

Cook Yield Procedure:

1. Restructured ham treatments were stuffed intol 1.4 cm x 76.2 cm ﬁbrous, un-stuck,
clipped casings.

5"

Stuffed chubs were weighed per treatment raw as a group, recorded, and placed on
smoke truck, one treatment per smoke stick, per row.

3. Place smoke truck with stuffed chubs in smoke house and were cooked to 70°C
showered with cold water to 54.4°C.

4. Remove smoke truck from smokehouse following showering process and allow ham
to equilibrate to 378°C at 20°C prior to weighing.

5. Blot dry ham casings with clean towel, remove treatment chub groups from smoke
truck and reweigh (378°C).

6. Percent cook yield was determined using the following calculation:

% cook yield = Wt. of cooked chub treatment group x 100
Wt. of raw chub treatment group

153

APPENDIX 12: TBARS Analysis

 

Rhee, KS. 1978. Minimization of further lipid peroxidation in the destillation 2-
tlriobarbutiric acid test of ﬁsh and meat. J Food Sci 43:1776—1778.

Tarladigis, GG, Wats, BM, Younthan, MT, Dugan, L Jr. 1960. J Am Oil Chem 37:44-48.
Zipser, MW, Watts, BM. 1962. Lipid oxidation (TBA) methods. Food Technol
l6(7):102.

1. TBA Reagent

Prepare the amount of TBA Reagent needed for your samples according to the
table below:

 

 

 

Thiobarbituric Acid Distilled Water Tog] Vol. Water and Acid
1.4416g 50ml 500 ml
0.7208 g 25 m1 250 ml
0.5766 g 20 ml 200 ml
0.2883 g 10 m1 100 ml
0.1442 g 5 ml 50 ml

Dissolve the Thiobarbituric Acid (Eastman Organic Chemicals) in the distilled water and
about 2/3 the total volume. Place ﬂask in sonic cleaner (several minutes) and shake
occasionally until TBA is dissolved. Allow reagent to come to room temperature then
bring to volume. Store in cooler, may be kept for 2 days.

2. HCl Solution

Make volume as needed; 1:2, HCl : H20 (v/v).

3. Antifoam (Thomas®, Swedeboro, NJ)

The use of antifoam may not be necessary depending on the product. Fish and
egg require antifoam while poultry does not. In this study, antifoam was used.

4. Sulfanilamide Reagent (Cured Meat Only)

Dissolve 0.5 g Sulfanilamide and 20ml Cone. HCl in 100 ml volumetric ﬂask. Bring to
volume with distilled water. NOTE: Store in dark bottle, will discolor with age.

154

Procedure:

1.

2.

Assemble connecting tube (spouts) and graduated cylinders.
Turn on condenser water.

Add 10 g of diced sample to 100 ml plastic bottle containing 50 ml distilled water
plus 10 ul antioxidant solution (Tenox 5 — food grade BHA+BHT).

Homogenize sample plus solution using Polytron mixer (PT-35, Kinematica, AG,
Switzerland) on speed setting 4 for 1 minute (Homogenized samples can be held in
cooler if needed).

Into 500 ml extraction ﬂasks, add 4, 4 mm glass beads (Fisher Scientiﬁc, Pittsburgh,
PA), homogenized meat sample, 2.5 m1 HCI solution, 1.0 ml Sulfanilamide solution,
46.5 ml distilled water, and 2 sprays of antifoam (Note: total volume is 50 ml + 2.5
ml + 1.0m] + 46.5 ml = 100 ml).

Connect extraction ﬂasks to distilling tubes and tighten heating mantles in place.
Turn powerstats to line voltage (setting 85) and heat ﬂasks rapidly.
Distill and collect 50 ml of the distillate.

Transfer distillate to 50 ml centrifuge tubes, cap and hold in reﬁigerator for TBA
reaction. (Can be held for 18 hours).

TBA Reaction / Spectrophotometric Determination:

10. Invert each test tube containing the 50 ml distillate and pipette 5 ml into each of 2

11.

12.

13.

14.

tubes labeled “A” and “B”. Prepare 2 blanks by pipetting 5 ml distilled water into
both tubes labeled “A” and “B”.

Add 5 ml of TBA Reagent into each tube containing 5 ml of sample and into both
blanks. Thoroughly mix each tube using Vortex mixer (American Scientiﬁc
Products, McGaw Park, IL).

Turn water bath on 100° C.

Place tubes in test tube rack and immerse into boiling water bath (model 9510
PolyScience, Sorvall Co., Niles, IL) for 30 minutes.

Turn Spectrophotometer (Lambda 20, Perkin Elmer, Norwalk, CT) to IDLE (must
warm up 20 min.)

155

15.

16.

17.

18.

19.

When the tubes are done heating in the water bath cool them in ice for at least 10
minutes.

Mix each test tube with sample for 10 seconds using Vortex mixer (American
Scientiﬁc Products, McGaw Park, IL).

Transfer sample to disposable 4.5 m1 cuvette (done in duplicates).

Turn Spec to ON: Manually adjust wave length to 538 nm for cured meat (read
samples within 1 hour).

Convert % T to optical density and multiply by the constant 7.8 (7.6 for poultry) to
convert to mg malonaldehyde/ 1000 g of sample, i.e. TBA Number.

156

APPENDIX 13:

2-Cycle Compression Settings

 

Texture Analyzer:

TA-I-IDi Settings:
Test Mode:

Option:

Pre-Test Speed:
Test Speed:
Post-Test Speed:
Pre-Travel Distance:

Compression Distance:

% Compression:
Trigger Type:

Data Acquisition Rate:

Attachment/Accessory:

TA-I-IDi Texture Analyzer
Texture Technologies Corporation, Scarsdale, NY

TPA

Return to Start

2.00 mm/s

1.67 mm/s

1.67 mm/s

24.5 mm

3.13 mm

Compressed to 25% of original height (75% compression)
Return

200 pps

-TA-30; 75mm aluminum plate, 10mm tall

-5 kg load cell
-TA-90; Heavy duty platform

157

APPENDIX 14:

Kramer 5-Blade Shear Settings

 

Texture Analyzer:

TA-HDi Settings:
Mode:

Option:

Pre-Test Speed:
Test Speed:
Post-Test Speed:
Distance:
Trigger Type:

Data Acquisition Rate:

Attachment/Accessory:

TA-HDi Texture Analyzer
Texture Technologies Corporation, Scarsdale, NY

Measure Force in Compression
Return to Start

10 mm/s

1.67 mm/s

5.00 mm/s

35.0 mm/s

Return

200 pps

-5-bladed Kramer Shear Cell

-50 kg load cell
-TA-90; Heavy duty platform

158

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

 

ocoz _ wcgooﬁazoﬁbsvaom oZ _ .05 boﬁobxm _ mom boEobxm _
252 £82an N wacwoo-£:oE\osEmom 282 3.3285 N ED bo> N com Eo> N
mount. m waumoo-5:oE\o=Emom 808,—. m E 3280on m com 382252 m
225 4 22882828282 225 4 an 2225 4 com 2225 4
88252 m wcsmoo-£:oE\o=Emom 88252 n >23. .m—szm m Ea: biwzm m
25... 2225 0 22895828282 2225?. 2225 e 23 222882 0 Ram 2288: 0
62¢. 388352 b w:_§oo-£=oﬁ\o:Emom 25855.84 388352 \1 >23. 50> N. 932 50> 5
88:22.4. m wcmumoohgsoEEémmom “58:328. w .83.. boEmExm w 3am boEobxm w
.8385 SauKKNQ M2-ueeé§e£§33§- mumﬁemé. 82:23:
3.-—2:55
hot/mm wccmoo

..to do 36:85 2308326632 $2223. $2623; 2923

8mm god 252

8:3— 8=£._:< 353.589 Ea: 3252:33—

 

ae=am _oaam rem—8w 6059:. "m— X—GZm—m:

159

 

APPENDIX 16: Trained Sensory Panel Treatment Randomization

 

Trained Sensory Panel serving order with random numbers:

Practice:

Trt 3 833
Trt l 679
Trt 5 930
Trt 2 249
Trt 4 614

Rep 3:
Warm-up Trt 5
Trt 2 318

Trt 1 403

Trt 4 927

Trt 5 715

Trt 3 423

Rep 2:
Warm-up Trt 4
Trt 5 372

Trt 4 116

Trt 2 888

Trt 1 505

Trt 3 182

Rep 1:
Warm-up Trt5
Trt 2 887
Trt 3 479
Trt 4 621
Trt 5 223
Trt 1 285

Treatment Key:
Treatment 1: 0.4% MC 1 / 0.6% KC

Treatment 2: 0.6% HPMC I/ 0.6% KC
Treatment 3: 0.4% MC I/ 0.6% HPMC I / 0.6% KC

Treatment 4: Control
Treatment 5: 0.6% KC

160

APPENDIX 17: TA-HDi Texture Analyzer Calibration and Analysis Procedures

 

Calibration Procedure:
1. Turn texture analyzer (TA) on.

2. Log on to texture analyzer program on computer. Program found on computer
desktop.

3. Turn TA key to the “run” position.
4. Clear deck of TA, removing all attachments and platform.

5. Attach calibration weight hanger attachment.

 

6. Turn TA key to machine conﬁguration.
7. Press “ENT (enter)” to determine load cell weight.

8. Press “ +/-“ to acquire appropriate load cell weight.
For example: 50 kg load cell will be indicated by “50” on screen.

9. Turn TA key back to “run” position and then back to machine conﬁgure. This saves
settings in TA.

10. Press calibrate key, then enter.

1 1. When TA screen reads appropriate weight put actual weight on TA weight hanger.
For example: 50 kg load cell will utilize a 10,000 kg weight. 5 kg load cell utilizes
a 2000 kg weight.

12. Press calibrate and when screen reads done switch TA key back to “run” position.

13. Remove weight from hanger but do not remove hanger.

14. Next, calibrate the computer.

15. Go to heading that reads “TA”.

16. Calibrate for “force”.

17. Press ok. The computer will then ask you to place weight on hanger.

18. Once weight is on hanger press “0k”.

161

19. The computer will then say “calibration successful”.

20. If this is not indicated or if calibration unsuccessful. Re-calibrate machine.

21. Remove weight and hanger from TA.

22. TA is now ready to analyze samples.

Analysis Procedure:

1.

2.

Once TA is calibrated analyses can begin.

Attach appropriate “attachment” to TA. For example: Kramer shear test attach
5-blade attachment to TA and from Gel hardness attach TA-10 attachment.

Create a personal ﬁle for data collection.

Open ﬁle with pre-deterrnined settings for analysis. Settings can be seen in
Appendices 6, 7 and 13.

Place sample in designated area.
Click on TA icon on computer screen. Select run test. Sample is then analyzed

Repeat steps 4-7 as necessary.

162

RECOMMENDATIONS FOR FUTURE RESEARCH

The results from this thesis have indicated future use of MC and/or HPMC with
KC as a purge controller. When used singularly MC and HPMC signiﬁcantly decreases
cook yields. Yet, when MC is used in combination with KC there is a deﬁnite purge
controlling effect shown by increased cook yield values and decreased storage day purge
values. Although this research was successﬁll deﬁning MC with KC as a purge
controller, future research needs to address consumer acceptability. Throughout Study II
off-ﬂavors were recognized by a trained panel in samples with MC or HPMC. Research
focusing upon masking the MC and HPMC off-ﬂavor intensity would be of great value to
the processor and consumer. One potential solution would be the incorporation of savory
ﬂavorings or sweeteners into the meat model.

Despite the fact that this research focused upon restructured ham products, further
research needs to investigate other brine addition options. Efforts should focus upon
making these brines solutions pumpable through an automatic injector. This would allow
the combination brine treatments to be injected into whole muscle meat products such as
beef, chicken, and pork making them more appealing to the meat processor. One such
research idea would be to inject MC with KC into prime rib or roast beef cuts to increase
juiciness and tenderness of the ﬁnal product.

Another potential research option would be to conduct a freeze/thaw study
utilizing MC and HPMC in restructured meat products. Kappa carrageenan has been
shown to decrease freeze/thaw purge, further research needs to investigate if the

combination of MC and/or HPMC with KC can further decrease freeze/thaw purge

163

values. In conjunction with this study a shelf-life study should be conducted determining
product life and microbial activity. This study could be particularly beneﬁcial to
determine microbial growth and activity with the addition of high amounts of water.

Study 11 results suggest the future research to determine if the addition of MC
and/or HPMC with KC has potential synergistic or additive purge controlling effects.
This study would have to be statistically organized to determine if the use of MC and/or
HPMC do have these potential effects. This study would be beneﬁcial as it would allow
a researcher to branch into new areas with the utilization of MC and/or HPMC in
processed meats.

In a ﬁnal thought, the investigation of MC and/or HPMC with KC exposed new
possibilities to produce high-moisture restructured ham products with little purge.
However, the basis of this new brine solution technique to be used commercially is
dependent upon cost. Cost determination is a research avenue that has to be confronted if
it is to become a new staple in the meat processors brine arsenal. If we can offer this new
technique as a cost effective purge controller it will be used in all segments of the meat

industry.

164

 

111111111 111 1111 11111 111111 11111 11

31293 024604