Chemi:cal Changes in Proteins

by ThermalProcessing
T. R. Dutson
Department of Food Scence and Human Nutrton, Mchgan State Unversty. East Lansing. MI 48824
M. W. Orcutt
Departmebt of Anmal Science, TexasA&M University, COllege Staton. TX 77843
Variousprocessing procedures are applied to food systems
[or preservation, quality improvement, and consumer con-
venience. These procedures generally provide food that is
satisfying, nutritious, economical, safe, and , convenient.
Thermal PTOcessing''S used by much of the food processing
industry to impart these attributes to its products, and many
different proceduies including cooking, blanching, pasteuri-
zcfion, and sterilization (1) are employed. Thermal processing
hl,f' both beneficial and detrimental effects on food systems;
tlwrefore, the food scientist attempts to optimize the benefi-
cia! effects and to minimize the negative effects of heat pro-
cessing (J, '2). _\
Heat is alsoone oftlte primary factors in the enhancement
of p'1latability of most foods, with many of the beneficial
changesrelated to food proteins. These changes
involve flavor and structural components; as most onsumers
will a3ree, properly cooked food products are generally more
palatabie than those in the uncooked stage or those which
have been overcooked. Other factors which must be consid-
ered, in addition to those of preservation and palatability, are
thc alterations in nutritional properties of proteins caused by
heating. Endogenous -enzymes found in many food systems
can produce 'either beneficial or deleterious effects on com-
ponents of a particular food system or on thll type of products
generat ed by a particular enzyme. Heating of foods generally
denatul'es these enzyines and pre-vents their action upon food
components.
\
Elfecls :>f Thermal Processing on Proteins
Maillard Reaction
One of the predominant reactions which oceurs upon
heating af protein foods is the Maillard reaction (non-enzy-
matic browning) which oceurs between free amine andear-
bonyl groups within foed systems. Although most free amines
and earbonyl groups have the capacity to -partieipate in
Maillard-t.ype reaet.ions, the major food substanees partici-
pating in t.hese reactions are the carbonyl groups of reducing
sugars ana free amino groups of proteins and other compo-
nents (3). Although the Maillard reaetion ean occur at ambient
and loweitemperatures, inere8sed temperatures have a
marked effect upon its activation. Recent reviews fully de-
o
, 11
C-H + HlN-R. ..
I
H-C-OH
I
sugar amine
R--r--r
!!
8H
1
H-C-OH

Schiff hase
scribe characteristics and properties of the Maillard reaetion
(3-5); therefore, only the salient features 01' this reaction will
be presented here.
Figure 1 shows the fiTst stnge o tho Maillard !@l:IcLiuJI,
which involves the production of a Sehiff base with the ear-
bonyl and amine groups. The Schiff base produeed by the
reaetion sequenee in Figure 1 normally undergoes an Amadori
rearrangement to produce a ketoseamine. Both the Schiff base
and the Amadori compound then undergo further reacti ons
to produce a wide viuiety of reaction prodticts which eventu-
ally produce the melanoidins responsible for the brown color.
A group of these reaction produets is presented in Figure 2.
The Amadori eompound arid its products have the capability
of participating in other Schiff base and aldol condensation
reaetions, producing a myriad of products which are difficult
to char.acterize in food systems (3,5). Much is known about
the chemistry of Maillard react.ion, however, its complexity
in foad systems in such that only a fraction of the total num ber
of reactions is understood. In fact, many of the reaetion
products resulting from Amadori compo\.lDos can cause
cross-linking between molecules, resulting in the formation
of numerous polymers (5). ,
Although there are many beneficial effects ofthe Maillard
reaction in foods, su eh as improved flavor (3,5), the 7-:: a(;,; ion
can also produce detrimenL'II effects in foods, primarily L: 0 1P.
a nutritional st.anclpoint; hOWeVp.T, jf the Maillard l oaction ill
foods is extremely severe, detrimentall1avors \ViII also ensu.
One of the possible adverse effects of the Maillard reacticD
is the reduction of protein nutritional quality through losses
in availability of specific amino acids, particularly lysine, (Jr
through development of toxins or mutagens (8).
Satterlee and Chang (8) have described the nutritional
changes induced by the Maillard reaction as follows: (1) de-
crease in the bioavailability of lysine, as well as several other
essential amino aeids; (2) decrease in protein digestibility; and
(3) possible formation of growth inhibitory and/or toxic
compounds. Figure 3 appears to eorroborate these statemerits
by demonstrating a reduction in the growth rate of rats fed a ,
browned versus control diet (5). On the other hand, according
to Hegarty (lO), if dietary intake of protein is high and if
sufficient quantities of the essential aminu acids are con-
sumed, the reduction ii1 protein quality due to Maillard-type
R-NH
I
CH
1I
COH
1
--
--
R-NH
I
CH,
1
C=O
; 1
l-amino1deoxy2-ketose
enol form
Ir
keto form
1
Figure 1, Proposed type reactlons Invo!ved In Initlatlon 01 nonenzymatlc brownlng. Adapiee from Paul (6) with permlsslon (John Wiley & Sonso Inc,).
) ..,
/- --,.
.1
N-subsllluled
alduhl'xosc + amine
i\
H e - N/
1I ""'-
C--OI
I
Til O 11
_r yllOIl
(J) .
Il
r
=N:::-_
. e-oll
I
CH
1
1l0l!
Il C=O
I
l"'-'O
(-
IH:
Ci l!() H
,
11
1
= 0 5-hydruxyrncthyl
../
7
,.,0 2-furalduhydc
c=o
H 1
11 . "::,,.'.'"""
<1 11
<1 e "... l,2'CI'I',UlllJ\ol
.<, ,-N"
(:=0


, '---....
1
CHOII
,
CHOH
,
,

CUl nUtlund
ell
11 '
C--OH
I
//
- /
(,; 11,
,/
c=o
I
eH
1 '
c:=o
C=O
I
lr
llOH
- c;;.= ==:. C-OH
L[ - Ol l
I (;'cnc thyl rt!duct o ncs
2,3-enediol
mclJyi nnd
cY-diclrbonyl (pyruvaldchyde. Rectol,
intennediate diacctyl, hydroxydiacetyl)
Figure 2. Sugar-amine (MalJlard) brownlng reaclions: Iwo palhways lo melanoidins and by-produCls. Adaptad rrofTI Hodge and Osman (7) wlth permlsslon (@Ma I
Dekker,lnc.). rce
30 0
1-
,
E 220 -
(JO
f-
J:
c:>
140 _.
.C

I

i
60 I
L-____ ____ ____ --L ______ L-____ _L, _ ____LJ
60 120 180 240 300 360
TI ME (days)
Figure 3. G-owlh curve Jor rals on browlled and cOlllrol diels. Key: browned. nlale
4 : browned, Jemale .; conlrol, male,A: anu conlrol. Jemale, O. (Averaqo 01
Jivo or six ralsin ea eh group; Ihe weighl gaills shown here are Jor Ihe ra:s which
""a Jed Jor 12monll1s. Ac1apled Jrom Kimiagar el al. (9) wilh pe,mi5s,on (@"
Agre. Food Chem.). ,-;, .
" '
';
may be 01' academic: inlerest only. tL mus1. W Ilul.ed ,
however, Lhat people 011 reslricted diets (i.e., l.he elderly ami
people f'rom lower income groups) muy be vulnerable to clp-
creased prulein nutriti9n in view (JI' the limiled varieLy of foods
they are.Jikely to consume.
o{ Proteins ,J
Thermal denaLuration 01' ]Jl'oll.eill occurs whell hydrogpll llild
other l1oncovalenL bomls, such ionic Hnd van der Wan!s
\onds, within the protein are disrupled by h.ril..l (i i). Thus,
the secondary and higher native-state sLruc:Lues of pr"{.eins
lire inLerrupted, chnn:ing lhe protein mm its naLve st.n{.(' {.o
an altered configurotio!l, 01' denolured staLe. i\ dilllf,ram (Vig
4) presented by Ledward (12) describes LruWiiLioll bdweell
t,he nntive ami denalured (predenaturaLional slaLe),
whcreby prpteins are abJe to inl.erad with olher compollenLs
wiLhin t:he system. Frorn the irilellllediale sLate oC dcnaturn-
)
304 Jeurnal ef Chemlcal Ec!ucotion
slalr.
Dcnalurcd
Dograded material
I j
1\ IIlL''''actioll ",i tb
\ pl.her co mpoll cn L(s)
\
Prl'<lcna luraLional
"tale(" )
l '""""'"" w'," " "' J
olher COll1pollcnl{s)
lncroasln.; telllpcritlurQ
FiyU!e 4. Thc Iransilion belweon Iho nalivo anu donalured (pro-denaluratlonal)
sIal" ,\tlapleJ JrUIn Ledwmd ( I:! wilh permlssion ( Ap.lied Sclenco Pub-
JiSt1lHS Ud.;.
tiOIl, am! clepending UpOIl tbe anwul1t of Lherma! perturbation
01' the nOl!coYDlen! within lile protein, proteins can
l'illler return f.o a nativ," sLaf.e 01' cunLinue to the denatured
:,ltI.{,. Frol11 the denaLured st,ut,e, provided sllfficient thermal
l!lIergy is supplied, proteins call conLinue Lo be dcgr;;-;:cd nr
rcad with ot,her componenLs within the systl!11l (Fig. 5), e.g.,
Lhe M;illard renc Li oll, I'igu re :1 delllOll sLrat.es Lhe changcs in
i'rolll c1issocinllOll Lo c!l'J;r;<!;[ion by honl.in!
.,: <id}"'-' :Il!. I.llljJcr;(I,re:" lid I.he "ssociuLed cllllnges in
pr"perLit,!; IJf I.ile prolei ....
'J'he thcrnwl sLaiJility nI' food prot.eins, or Lhc umoullL of hcaL
denatllrntion, is markedly I.1ffedcd uy Lhe protein's environ-
n1l!nt, fiUC\l m the UlIluunt oC water fls80ciated with the protein
I
I
!
I
,
i
I
1
I
!

-1
I
-.
Pro perty
Subunit
Viscosity
Hydrntion
Gclution
(following
heating)
I-! C/lLlIlg Lplllperll Lure ( OC)
; 00 120 1' 10 Hin
... _._--- - _._-_._------_._.-------_._--- - - ------\- --
dis80ciation-unioldinr. _ _ .. _ __ . _ _ _____ de!(r:ldlll.ion
dccrease-precipitati(ln _ __ __ . ____ _ in crease in solllbilil.y
increa1<e-decrcasc __ __________ decrcnsc
increasc _ ____ _
dcerease
regulur _ __ hard-frngiie
50ft clllsLic
___ sol
nu l urnlion 01' bovine serum
a lbumin (ESA), lale ral asso-
ciaLion of p rotein 1l10lecules
occurs through a chain reaction
of groups wilh di-
sulfide groups (J8). Kolthoff
and Tan (J 9) found that heat
dena luration of BSA is not re-
versible in lhe abscncc of a
sulllyuryl binding agenl but
Lha L heat d enulurulon s re-
versible when thc sulf11ydryl
groups are protccted.
, FIQlI'e 5. l11e changas in protelns !rom dissoclation to degradation due lo heating al different temperatures and aSSociated
cnanges In the propertlcs 01 tho prolcms. Adaptad Irom Kinsalla ( 13) wilh perrnission C@.J. Amar. Oil Cham. Soc.).
One o[ lhe milk proieins
({3-lactoglobulin) is thermally
very unstable, und Lhe stabiliLy
of milk proleins is affecled by
(14). Tropocollagen molecules in soiuUolI huve a
temperature 01' abouL 370; whereas those sa me 11J()l ecules.
whenorganized into cllagen fihers 01' cOllncctive tisslic. have
a denaluration ternperuLllre of about 60C (12). III()rganic
ionic strength, pH;-typc of solvenl., [llldoLher f'aH+lfs also
have aneffcct on lhe t.herrnal s!.abilLy of pnlLeins (l.).
the noncovalen,t. bonds wiLhin cach individual protein are
c1ifferent, each prolein reucls cJifTerelllly lo thermal cnergy,
und each proteill is affect.ed different.ly by t.hc some: !. ype Df
components in Lhe foocl system (12,1(') .
. .
,
A ggregation, Precipitation, GeJation, and Degradafian
In food systems containing several diffecenL proLeills,
thermal processillg causes amllg_ proLeins and
protein-prot.cin inLeract.ions. be vcry
important in determining the properties of heuleu [ood. AI-
t.bough the exact mechanism for amreglltiqj1 of proleins
during t.h)rl1)al processing is not clear , some type of covalent
bonding must be involved because 01' the 'stability of mosL
prot.ein aggregates (12, 14). .
Depending upon the [ood system utilizad and thE) .. compo-
nents within that [ood system, tbenhal prQcessing.crproteins
can proceed beyond the agggation sLage apd"cause precipi-
tatioll and/or gelation. Normally, wben protein preclpitatiol1
(l ecurs, there is a decrease in waler-holding capacity and n
recJuction in the functional properties .of proLrins in mosl [ood
systems. However, when gelation ocCurs, Lhere may be un in
<::rease in water-holding capaeit.y of ti,., f,-,-xl fiyslern by en-
lrapmenl of waler within the gel rnatrix (12). When nll in-
crcasing amoun(. (JI' tiJerlllal energy i!' applied l." pro\.ein sys
tems, degrudat.ion including deslruclioli o' mino
.lcids, hydrolysis (JI' pepLide b()nds, Hnd o\.he1' r<:HctioIlS.
Accoreling lo Neucere und Cherry (14), excessivc leal.
treatmenL causes pro(.eins lo undergo mallY COlllpJeX rpucti"lls
which c1ecreuse Cheir As s hown in Tabif J .
Coking in boiling wat.er, hy bo\:h conve nCiollill ,lIId ;ni (:rowi.IVP
means, the illll()UII (. 01' arn lno lci(h; in peas (171 .
MicrowBve cooking \Vas found to be more des [. nlcl.i vl'
to . amino acids t.hun conventiollal cooking b\l t lJ rod\l cec
slightly grealer reienol1 ofthinmin and riboflnvin (J 1). 1'his
indicates that more res61arch is 011 the type ano alllount
; of energy absorbed relaLive to nutrienl conlent 0I ihermall."
processed foods (J 4). ,- . ,
Other Thermally Induced Protuin Reactions
In addition to the Maillurd reactiol1, Lhermul process 1lJ.(
causes other reactions to occur in fOlld proteins due Lo t he
un[olding of the prot.eins during dcnaturation and the modi -
fication of protein side chains. These reactions inclucle: di -
sulfide bond formation und hydrogen sulfide lberat.ion; iso-
peptide forrnalion; raeernizaliol1 nf nmino ncids: ami ulLeralion
{e enzyme acLivitiC:l with Lhe [oud systern.
Disu/fide Honds and Hydrogell Su/fideo During' hea t <-le-
. . . Lhis lherrnnl insl a biliL:( of
J-I:JC LogJouu ll n (UJ. However, when (:i -lucLoglobuJin is hcuLed
wi lh K-casei n, a d isulfide lin kuge is formed , which reduces lhe
denaturation ami aggregalion 01' J-lactoglobulin and, hence,
Illilk proleiml (2/). The fundiollllliLy 01' Illilk powdor!l in bread
illl(l hilkery producls Ilw; been illcrenscd hy warming Lhc milk
,erore POWd l' !' prot!uct. oll (.0 prollloLe lile JI!lultlJe IllIk:ge
helwcen {3-lnctoglobullll llIld h-cilsein (1/).
'rile 01' disulriele bonds in meu!. pro!.eills occurs
be L\Vee n 70 o; ,d 1 wit.h 11 concomiLanL dccrc use in t.he
11\1111 ber 01' sulll lydryl 'fi Je ('orma Lill n 01' el isu lfi Lle l)onds
iJl :l l ea t: pr oLt! ins is lI()l likel y cause 0 (' cougul nLio n of' lile
pr() t. ciw, since c(IIl gul nLi ol1beg ins Lo occu r aL 45C; howevcr,
t. he f'ormalioll 01' bonds lIluy be relnleu to oLher lt!x-
t.ural changes occurring in med.s uetween 70 ane! 120C (22,
2:.1). When porlions of meaL are heuLed for long perio(]s of time
ul temperutures subslanliully ubove HOoe, lhe sullllydryl unu
disulfide groups in lhe meato proteins are almost. completely
lost. This occurs by oxidalion Lo cysLeic acid, or by lhe splitt.ing
off of hydrogen suJfide. The muj ority of lhe hydrogcn suiCide
originates [rom f,u!t11ydryl groups on the proleins and in-
creases rapidly wiLh incrcasing temperaLure (22).
!sopeplide FormalilJn.. The formation of if,opeplides by
cross-linking of peptide chains is increased at higher tem-
peratures (8, 14), producing some of the following products:
lysinoaJanine; lanLhionine; and ornithinoanaline. rrhc!le
producls ha ve becn demonstruled lo reduce the ability 01'
proteolyiic enzymes Lo cleave proteins (8) und Lo reduce lhe
Table 1. Ef1ccl 01 Cooldng on Amlno Acld Conlonl 01 Colossus
Peas .
Arnino
lr. id

sI

I\spur;:t9ine
Glutamine

Sarlna
Proline
Glycinc
Alanine
Cyst ine
Valine
Metionine
Isol euci ne
L! ucine
Tyrosine
Phon.ylnlanino

O.IHl
1.'11
2.9<1
4.46
1.04
1.41

0 .93
1.09
0. 11
1.3 1
0.23
1. 16
2.13
0.74
1.53
Concunlration-- .g/100 9 dry wt
Cool<od----
I
Convcnt ional Microwovo
._--------_._-- --
1."12
o.no (i .01
t.:I5
1.76(6.1)
4.20 (5.8)
0.98 (5. 8)
1.35 (4.2)
1.05 (3.7)
0. 89 (4 .2)
1. 04 (4 . 6)
0. 10 (9. 1)
';.26 (3.8)
0.22 (4.3)
1. 09 (6.0)
1.01 (5.6)
0.70 (5.4)
1.47 (3.91
1.68 (l.l)
rus e 12.DI
1.20 (8.?)
1.67 (9. 2)
4.05 (9. 2)
0. 94 (9.6)
1.28 (9.2)
1. 01 (7.3)
0.03 (10.7)
1.00 (8. 2)
0.09 ( 18.2)
1.20 (0.4 )
0.20 ( 13.0)
1.07 (7.0)
1.90 (7 .0)
0.68 (O. t )
1.40 (8.5)
Vti/uos in pi:\ rOfllhesi s (i,0 PQf cent los$os. Adaptad 'rom Ctu-.g el al . ( ti") wlth purmlG$;o.,
(!:JJoumaf al Food Scionce). .
Volume G 1 Nurnber 4 April 19134 305
Table 2. o-Aspartlc Acld (o-Asp) Content of Commerclal Foods
and Food Ingredlents '
Product
D-ASpR
o-Asp/L-Asp o-Asp + L-Asp
Texturized soy proteln
0.095 0.09
Baby formula (soy-based) 0. 108 0.10
Simulated bacon (soy: based) 0. 143 0. 13
Corn chips
0. 164 0.14
Dalry (caseln-based) 0.208 0.17
Relatlve ,atlos ", total aspartlc aro its o- aro L-<lnantlomers (o-Asp. L-Asp). Adapted
I,om Satterlee pro Chang (8) with permlssion (Americen Chemlcal Soclety).
absorption of S?me other amino acids (J 4) . Isopeptides are,
therefore, to nutritional quality, but they may
have a beneflclal effect on the stability of the protein matrix
of sorne food systems.
Racemization 01 Amiho Acid Residues. An excellent review
has be en published recently describing the effects of amino
acid racemization on the nutritional quality of proteins (8) .
-- Aeeofdig to Slitterlee a.nd Chang (8), a portion ofthe amino
acid residues fouhd in proteins which have been treated with
heat and/or alkali is racemized. This racemi zat ion occurs in
many common foods, and reduces the nutritional value of food
proteins by decreasing their digestion by proteases. Both the
absoprtion of D-amino acid residues and their subsequent
conversion to' the L-enantiomer are slow. One note of caution
as pointed out by Satterlee and Chang (8), is that sorne of
observed racemization of amino acids may occur during pro-
tein hydrolysis in preparation for conducting amino acid
analysis (24) .
Table 2 (8) presents the amount ofD-asparticacid present
. in commercial foods and food ingredients. For those foods
presented, the D-enantiomer comprises between 9 and 17%
of the total aspartic acid in those foods.
Enzymati Reactions. Al! raw materiaIs destined to become
foods, or parts offood systems, contain endogenous enzymes
whi ch can have either beneficiar or deleterious effects on the
resul ting food. Many [ood syst ems al so contain added, or ex-
ogenous, enzymes from various sources which, when properly
.....-" controlled, have tremendous beneficial effects upon the food
, sys tem. Many of the enzymeS present in foods are proteolytic
in nature and, by their action upon food proteins, can a{fect
the resultant food product, again, either benefi'cially qr de-
,-... trimentally.Enzymes in rood systems can be activatedby
exposing the food to temperatures near physiologicaI tem-
peratures, and enzymes can be destrqyed by increasing the
temperatureof the food $ystem to a point where the enzyrne
is irreversibly denatured (14). A!though many components
within the food system, in addition to temperature, have an ,
effect on an enzyme's activity (such as pH, ion concentratian,
and inhibitors), temperature control can be used, alone or in
combination" with these other components, to control more
effi ciently the protelysis of food proteins.
An example ofan exogeneous proteolytic enzyme used in
a food system is the addition of rennet to milk, where its action
on the protein casein aids in the curd formation of the
cheese-making process. The proper tempera tu re is very im-
portant during the curd setting period and affects the rate of
formation, firmness, elasticity, and other properties of the
curd (25) . The proteolytic activity of rennet in the resulting
cheese whey (a by-product of curd formation) can be detri-
mental, since dried whey proteins are sometimes used sub-
sequently in :other rriilk products which contain casein. Galf
rennet is more susceptible to heat denaturation than fungal
rennets, and; therefore, whey which contains calf rennet is
more useful Jor incorporation into casein-containing dairy
products (26). '
The protelytic enzymes contained in muscle that degrade
muscle proteins and increase tenderness (27) are an example
306 .Iournal of Chemical Education
of an endognous enzyme system having an effect on a food
system. Activation of these natural proteolytic enzymes can
be accomplished by high temperature conditioning of musclc
during the early postmortem period, resulting in an im-
provement in the t enderness of the meal (28, 29) . However,
when th.e meat is cooked ar high temperat ures, these enzymes
are rapldly denatured, so very little t enderizaLiol1 occurs
during or after the cooking process. '
Eff ects of Thermal Processlng on Prot el ns of Speclflc Food
Syslems .
Due to the number of food systems which employ
thermal processmg ll1 sorne form before constimpLi on and the
effects o.f heat ?n p:oteins i'n many of these systems, a com-
prehenslve reVlew lS not possible with in the scope of t his
papero However, a few examples of the effects of heat on
proteins in the major food systems and t he resultant im-
provement or decrease in quality should suffi ce t o illustrat e
the importan ce of thermaI processing control on food proteins
and ultimate food quality. These examples will also iIIustrate
sorne of the reactions previously discussed that occui' in food
proteins duc l0 lhermal processing. The reader is direded to
reviews by and Kvale (30 ) , Pri estly (31) , Fox and
Condon (32), and Cherr y (33) fo r more complete discussiol1s
of this topie. .
'-Muscle Foods
Since the proteins within skeletal muscle of red meats, fi sh,
and poultry are quite similar, and, since thermal processing
affects these proteins in a similar manner, the interaction of
heat and proteins from aU muscle foods will be di scussed to-
gether.
Denaturation of myosin (the primary myofirbill ar protei n
in ui usde) and sarcoplasmi c proteins occurs ,to a large ext ent
between 40 and 70C, as shown in Figure 6. Associated with
the denaturation of muscle proteins is a hardening of the
tissues and a release of juice (22). Figure 7 demonstrates the
effect of heating on meat tenderness (shear force value). This
figure 'ilIustrates the toughening of meat (increase in shear
' force value) between 40 and 50C, whi ch corresponds to the
temperature of the most marked protein denaturati on (Figure
6). Littl etougheni ng occurs between temperat ur es of 50 and
65C, but a furt. her incr easl? in tough n ess b l? t wl?l?v GS
and 75C. This second phase is c10sely associated with coll agen
10 0
80

"
:?
g 60
...

Q)
40
"
o..
20lL __ __ jl ____ __ ___
20 40 60 80 100
CooklnQ temperatura (OC)
Figure 6. Myosin and sarcoplasmic prolein denaturation and colla gen shrlnkage.
Curve 1, percentage denaturation 01 myosin in the myolibri l. Curve 2, percen:age
denaturation 01 the sarcoplasmic proteins In the muscle. Oblong horiiontal area.
the temperatura zone 01 c ollagen shrinkaga. Adapted Irom Davey and Gilbe,t
(34) with permlssion (@Blackwell Sclentllic Publications Ltd.).
shrinkage (34,35). The toughening of the second phase (hc-
tween 65 ond 75C) may a lso be affected by los8 uf juice on(\
the formation ofnew cross -linkages in the coagulated rn yofi.
b rillar proLeins (22). The decrease in shear force (improved
tenderncss) whi ch occurs abovc 80
0
e may be associatcd with
the degradation of cross-l inks wiibin the myofibrill a r prolcins
as evidenced by lhe production 01' hydrogcl1 suICide from d i-
sulfide groups in this temperature range (22) .
Egg Proteins
Eggs have been used in many food products oecnuse 01' lhc
functional propcrtles of holh egg white a nel yolk prol.eins
(36:"3.9). Sorne of the more familiar food procluds \yhich, in
order to make use of these functional properties. incorporate
egg proteins are: cllkes, mcrin,;ues, souf!1cs, clIt:;tards, etc.
The beneficial functional properlies ()f egg prol.eins me clue
Lo their dcnllluration ami coagulal.ioJ1 aL s llt' cil'ic
.and the formation of u st.uble malrix upon cougu lulioll (111).
A majority of egg proLeins coagulul.e 1H'!WCl'll l ; tl :1/ 1.1 ''( [,0('
(:36-39); however, lhe conglllalioll lellljJt'r,1i.1Jre is ;lill,clcd hy
plj and salL.collcelltraLiol1. as would 1.1' cXi,, ttcd :, ill(,(' s:lil. .1I1t1
pH a lLer Lhe hydrogc n bonding p r"Lei " ".
Hydrogen s ulfide. produccd fr olll bul h sult11ydr y l {nd di
sulfide groups wiLhin t h e (40), to be rel " ",(, d
when e{1i products are heaLed Lo tcm[Jc raLures el< ccecling
GOoe. The green color [ormed ()J1 the surface of th" yolk 01'
hard-cooked eggs is a resuit o( hydrogl,n liber/l Lion
from albumin and its interact.i o n wiLh iroll i' rolll l he yolk (<JO).
This green discoloration can be r ed u ced by conLrolling Lhe
temperature o(heating a nd subsequenL cnoling.
Fruits and Vegetables
Enzymes cornprise one llf' the protein comp<,nenLs 01' fruits
and veget<Jbles: if the activity ()f these e nzymes is not limited,
a reduction in the.quality of the food can ensue. Phenolase is
one such enzyme and is r esponsible for
of fmit and ve{etable p roducts (4 ). l'er(\ xidase,'tlll0Lhe r en
zyme present in fruiLs /lnd vegetllble8, can lcad Lc reducliun
in nutriti on. color. and f1avor of the fruit nnd vegeta bl e foocl
systems (41). Phenolase is relatively unstabl e Lo heat. and can
be inactivated by a mild heal treatment, whereas peroxidase
is much more rcsistant t o heat and needs higher tempemtures
1'01' its destruction (41,42) : These two exan;pies illustrale the
effects of thermal processing on enzymatic proLe ins within
,o
v
:>
'O
,.
"
JO
,.. 'p.
-r ./ . l
."
.2
..........,;..-J.. J. -
i .
(;
JO T
.,
.<::
<f)
20
Cookinll
Figure 7. The two-phase elleet 01 cooking tempflrature oro va!ues.
Standard devlatlons are glven by vertical lines. Each point is tho moa n 01 8-16
delermlnatlons from tha musGle 01 lour bulfs. Adaptaci Irom Davey and Gilbwt
. (34) wllh permisslon (@Blackwell Seientifie Pub!icallons Ltd.).
foods ilnd how specific control of these enzymes lhrough se-
lecLi vc denatu ra tion nnu coagulatioll may improve the QualiLy
of t he food p r od uct.
Cereal Grains
Uuring t.he mixing 01' bread doughs , thiol tlisulfidc inter -
change reactions are important in the development of desired
elasLicily of the protein lTlatrix of Lhe doughs (J 1). In additoll,
activiti es oC Lhe amylase enzymes are extremely importllnL for
lhe propcr degTil da l.iol1 of s t urch wi\.hin the dough maLrix and
fo r the p roduc tion 01' malLose r equired Cor Lhe acLion of the
yeasl (41. 4:J. 14). Tempera\.ure cOlll rol is essential 1.0 propcr
dougl1 develo pmenl: in order to ensure proper act ivity oC
amylHse em:y mes, and proper development of bOlld inlerac-
I.iol!s betwecll t,he elasl.ic (iut.en proteins, tempcrat.ures must
be all.ered depelldin.( upon lhe relnl.ive (;Ollt.ellt of enzymcs ami
llld glul.e ll in I.h(, dough (.l.:!). .
l)uring or lhe bread. mi lelllperaiure rises, yeHs l
; u' L!vi t ,v illl,, ' f( 'i \Sl':i 1Il lt. l ()\ :C\lrs nCi l1' :)11C. At allolll
j;)O ( : . s; rcl gr \lllu l es (1) Lhe un) .\',
l'I s t: .' ; l." :d.l.ilc k Lhc sl.ilr,:I, lllllt.eriill illH! produce I.h e proJ>l'r
,,tll'll Ct>II SISl. cIICy. /\llIylil."C t.:II/.ylll(:S Ilre illllcl.ivlIl.ed 111. IIJI '
prtl." I 1Ii1I.el y '/ [,oC. , 1. wlli c h I.lllll l.I ll! glulellllclwork Illsl>be-
l:ins l." dena iure and l:oaglllale. Curtg u.laliol1 conlinucs up lo
I.hc poinl nt. which baking is complel.e. al a temperalure of
JOOC \'jJ, ,14).
Tlte loa l willl'l.'ilcll tCII!Jleral.ures o!' J ;)()-lGIlC: ami
ch" col,,!' llld CllIVOr ,,1' che Cl'usi. ''''c parlially ti result uf lhe
llcc urn.'nce 01' :\llaillard type reaciip ns al Che bread surfllcc U,'J .
H ). 'fhe lengl. h of timc lhe crust is Illainlai 'l cd al l.h ese high
l emperatures d e termines the exl.enL 01' Mai llard reac Lion ami
lhe lhickness of the crust. Maillnrd reuctions ore also impor-
tant in s ome speci al bread producls, s uch as German p um-
pernickel brcad, where the extrelllely long baking time nt in-
termediale temperaLures produces appreciuble quant.ities of
sugars as o consequence of amylasc acLiviLy. The reaction of
l hese sugurs wiLh nmino groups in Mll il iard-lypc renclio!ls
produces 11 very hard br ead \Vilh 5peciaJ flllvors (43). As a rc-
sult uf t he large amount of Maillard-lype reucl. o!1s, lhe prote in
value o[ this bread muy be reducecl .
Llterature Clt ed
(1) I.unfl , 1). U . 111 nI' Fuod !"cit!l)cc. 11. uf FfHld
ioll." F, nrulnn . O U-'. .. (.,. 1,.(.', \ NI'l\\' Yurh. 1f171i. (l.
I ,!' Th; jS:'i f!ll, H. A. C" une! Krrkhor, P. tI. A. M" 1.' 1 "Ph""it'nl. Chf'IOicnl r!IH! Binlo"/I
Chu!); !!!-' in io' P( ld rnu'4l'(\ hy Thl"r 111 11 I (r:d,I"",: Ht) yem. '1' .. AIUI
(l.) J\Pldll' d SCIt'IH:'" Jlllhli:-;hl'r:\ .td., 1,01ldoll, 1!177, p. 11l .
CH H. F.o IIIHI !\ . . 1 .. itl (' III:/IIi(,1I 1 111111 H: I:II:,cIII ( : hIIII! I'"
i n Fnnd Cn usf'd 1,\, T ht'fllwl P r lll '1'1'Is illl:." /;d,tllr." II"\Yl' r:l, '1' .. "oHI 1< \' hlt" (U. 1\1'
pl j(.d St' lh f' P(d;h." h"f :i 1,1 d , I.Hlldllfl. I p. lI iH.
(.1) ;rih';llll . C .. tFcli lurl. "tyl/1illllfll 1(I'1I (' li' , II S in Fund. " Jlr .. c 111 1. S:-'lIIp .. llfhlp\' ull" .
I'p rr !1I1Hlllln Jlr" .';s. I h: lnr d , 1 l . ji
Ir,) F"ll1r.- v , IL .:, . II IU\ \ Vh. IHk.'r ,.1. H .. I'r,II .ill i 1 lI ' rl n /alillfl , 1111, 1
F\l JI'r t (J.;tlil 1" , ! I,.'fl y . i. I' .J. ,\/I'I'T. ( " " ' 11'. S UI' Sylllp. '201), \\'1;:- 111111:11111
pe. p. 201
lIi) j'IUII, 1' . (' .,;" " }' UfI.J 'l'1"'<lr;.' 111\11 A l'lIhnllu,,, .... ' I}'.II.lm . .- "It"1. p, e .. "1111 1 ',,1 "\1' t , 11.
H.I .john Wilcv &. .sonli, hu'., NI ' w Yllrk , IlJ7:.!. p. llO.
\'/ ) K, II llci' O"mRI1, E. M" in " Prillplt'!lII( F"tI(1 S"It'!H'l.1. Fu("1
II-:di tur: "'Cll llt! ll1ft . O. IL). Mllrnd n('kkN, In" " N('w York , IlJ71i,1' , M,I.
!HI Sn!lcrln!. 1.. I J., nnd ChI1l1 l!, 1\. C .. "1"0,111 Pr kin J),'ll'rlu rnliClIl: Il/Id
( Eu i lor: 1'.). A /l wr, CIIl'IIl , SO(:, SYlIlp. '.!. )() . \ V:I:>hi l1.!l ol1,
n. e. , I p. 109.
I!I) M .. 1.cc, T.-C., Chiehc, .. ln. e, O. , ,). 1' ,I.'f! ('. FII"d (' '' ,m., 2R. r,(} (I !JHO) ..
(ni P. V . . 1. , I I " Food Prot('ill!\," (/Ji lor ... FIIX , P. F .. !l nd C:I II HlolI,.1. ,J.). Apl'lll'"
S,it' IH' t' Pu hli :>l ll: r!-ll. !d" Lont!PII . I !JXI . p. ]1:).
I 1 J . . J. ": .. ;" "Font.! I' rnt cinll ," U ..'dil"r,.,; p, f .. IIlI d Cundnn, .J. .1.). Applit\
S(:ie n(" t' 1. t<I. , l.onc!ol'1 , 19R2 ; . [.1. ,
:, 1 Lt'dwnrd, n . A .. i" " Efrf!;Ui (Ir Henli".: on PricJoIllcy. H, ,J.), AflPt.l'
S(' icll. :(' Pl!hl ir;hf'tli I.td., tondun, 1979.
( 1;1) Kins(' iln. ,1. J':., J. Amer. Oil Che!n . ,'-;11(' " 5fi. :!,1 2
(14) Nf'lIt:cre, .1. N., Rnd Chcrry, ,1. 1'" i n " "'1",<1 I'rolcin ()t' ll'riurntilln: Mf!t:hnlli
s
,."" 11111..1
FlIllc lioIHt l ily," (f:dit , If: P. ), Al1l e r. Chell) . Su(. Symp, 'Oti.
ne, IIJH2, p. I :j[.
\ I :,) Finc h, A., nnd l,cd wl1r d, 1), A . j jwfh im. /I ;"p"Y." I\ (' tu, Z!,I; (nJ7; I).
( Hil T lll dord. e .. " du. Pro/ r C/um. , l.:!. 121 tl !)ll'H.
f 17i S. Y. , Morr , C. U., nnd .Je n , ,J. ,1" J, f'""d SI'l.. 46, '27'2 11HHIl.
t I MI H. C .. !! ud ,Jcnsen. Jo:. B .. J. Anu'r, Chot! , Sur . , 7!l, 2: mO (1 9,r)'I )'
! I!l) I( pll h"rr, 1. 1\ \., ,lid '1' 11 11, B. 11. , ./ , Afil a . (:11(' 11 1. H , 'l717 (196.'i ).
('.?Ill I k\Vilt. ,.1. N., Nr /h , Mi O. (l II rI ()o;r )' ./ . Jfi. ,17 (I !JXl) .
l'1.n Morr . C. V., J . "nir.\' SCI. , 5R, 9'11 . ..
u :n HIIIllIII , H .. 1,1 "Phypi c"' .f.1wtnic:ulnnd Biolol:it'lll ChunnlA.'" CIHI!'(d '.' )' I
HcJ)'CIll, T., ROO KvAlc, O.), pphl'<1 Sr. ,tnct' Puhlul.ht'rK Ll' l..
l.ondnn ... j!I77. p. 101.
.n,.i l 10nA