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Reprinted from CEREAL FOODS WORLD, July 1979, Volume 24, No.7
Published by the American Association of Cereal Chemists, Inc.
3340 Pilot Knob Road, St. Paul, Minnesota 55121
Printed in the U.S.A.
The functional properties of proteins in foods, including emulsifier. This versatility reflects the fact that the 21 amino
those in cereal products, are determined by the molecular acids have different side chains tied together in varied sequences
composition and structure of the individual proteins and their and amounts. One protein may contain groups that form
interactions with one another and with other substances. associations with polar substances and groups that favor a
Improving or modifying food characteristics such as viscosity, nonpolar environment.
texture, water absorption, or fat emulsification may involve
altering the constituent proteins or adding other proteins.
Excellent reviews and symposia have related many aspects of TABLE I. Functional Properties of Proteins in Foods
the chemistry of proteins to their contributions to the stability and Their Applications
and organoleptic properties offoods (1-3). However, use of new Property Applications
techniques such as amino acid sequence analysis, x-ray Emulsification Meats, coffee whiteners. salad dressings
crystallography, and NM R in the study of protein structure and Hydration Doughs. meats
physical properties is advancing our concepts of the roles of Viscosity Beverages, doughs
proteins in food processing, structure, and acceptability. Gelation Sausages, gel desserts
Table I summarizes some important functional contributions Foaming Toppings, meringues, angel food cakes
of proteins to foods. The role of proteins, such as those in Cohesion binding Textured products, doughs
dough, may be critical, even though protein may be only a small Textural properties Textured foods
Solubility Beverages
fraction of the food product. Most of the examples in this review
are based on studies of proteins in cereal-<:lerived foods, but the
basic concepts generally apply to other food systems.
Most plant tissues used for food are storage organs, such as
seeds and tubers, where proteins and carbohydrates serve as
reserves. In developing endosperm of cereal grains such as FuilctiolIlI Groups Disrupting Solvents
wheat, most of the proteins are not dissolved in the cytoplasm Bond Type IlIvolved
but are deposited initially in storage organelles, membranes, PIlysical
and other subcellular structures (4). To facilitate their compact E1ettmtJ1ic Carboxyl Salt Solutions
deposition in storage bodies or their insertion into membranes, -CQO-····+NH 3- Amino Hiib or Low pH
seed proteins often have unique compositions. Usually such Imidazole
proteins are modified enzymatically after their synthesis and
Guanido
transport, thus accounting for some of their unusual solubility
and structural characteristics (5). lIydroi!ll IlolllI
One protein may serve both as hydrating agent and fat - C=0...HO- Hydroxyl Urea Solutions
I Amide GualIidille lIydrocbloride
. NH ~~~ ~~l!~~~~ _
1 Presented at the AACC 63rd Annual Meeting held in conjunction with Hydrophobic Bonds Long Alipllatic
the Sixth International Cereal and Bread Congress. Winnipeg,
Manitoba, Canada. September 1978. 0-vvvv Chains Detergents
l Mention of firm names or trade products does not imply their /V'V\./\.-O Aromatic Organic Solvents
endorsement or recommendation by the USDA over other firms or Covalent
similar products not mentioned.
Disulpltide Bonds Cystine Reducing Agents
-$-$- Sulfite
This material was written by Federal employees as part of their jobs and is Mercaptoethanol
considered to be in the "public domain" and not copyrightable. Fig. 1. Types of bonds between protein chains.
.--
proteins is clearly illustrated by the difference in solubilities of
the genetic variants of the milk protein f3-lactoglobulin. These E...;;-. . ._----r..;.;,,;;..;.;..:--.-
100% B
proteins have the same shape and size. As shown in Fig. 4. f3-
lactoglobulins A and B vary by only one charged group. but "'"
~ 0.5 / "". ,
75% B - 25% A
their solubilities in aqueous salt solutions at neutrality differ
considerably (IS). The two proteins associate with each other by
~
=> £:_0
.P':........ o - o - - - - o · o
50% B - 50% A
0-------
electrostatic forces. as shown by the solubility curves of A and B c ,&::::~- ..__..__-.;,I,;.;OO;.;"I..;..o..;,A;.... .._
mixtures with solubilities intermediate between those of the : 4')r;."-
pure proteins. Wall and Beckwith (16) demonstrated that the "- aa
solubilities of mixtures of A and B are a function of the amounts 0.5 1.0 1.5 2.0 2.5 3.0
of each protein in the solid. the solubility of each pure protein. Total Protein, grams/lOa ml
and the amount of salt in the solutions. Of course. if the pH of Fig. 4. Solubilities of {3 lactoglobullns A and a and mixtures of A
protein solutions is made more acidic or basic so that negative or and a in 0.00625 M NaCI. {3-lactoglobulin A differs from a by two
positive charges predominate. the proteins will be highly soluble amino acid residues.a. contains alanine and glycine. A contains
due to charge repulsion. valine and aspartic acid. From Treece et al (15).
Many proteins. especially membrane proteins, remain The role of intermolecular disulfide bonds in functionality of
associated even in the presence of strong hydrogen bond- food proteins. especially wheat !lour doughs. is being critically
breaking solvents such as 8M urea. Various surfactants such as reevaluated. Rheological properties of dough are generally
sodium dodecyl sulfate (SDS) or salts of fatty acids can disrupt explained in terms of either rather extensive intermolecular
the hydrophobic bonds that unite these proteins. Kobrehel and disulfide crosslinks (27) or fairly linear concatenations of
Bushuk (22) reported that wheat glutenin disperses well in limited disulfide-linked glutenin polypeptide chains (28). Based
sodium stearate solution. During gel filtration chromatography on the increasing importance attributed to hydrophobic bonds.
on agarose columns. glutenin behaves as if it consists exclusively some workers now minimize the need for extensive
intermolecular disulfide bonds. Kasarda et al (29) explain the
action of reducing agents on protein properties as the result of
conformational changes in the proteins after disulfide cleavage.
During gel filtration chromatography. careful fractionation
of proteins dissolved in dissociating solvent provides evidence
that a range of protein species. differing in type and extent of
disulfide bonds. exists in plant seeds. especially endosperms of
cereal grains. Most globulins and gliadins and possibly some
wheat glutenin proteins have only intramolecular disulfide
bonds (Fig. 5). Most acetic acid soluble glutenin molecules have
Albumins and
Globulins
Gliadin
Salt Solutions
70% Alcohol
6
+ S's
SH
. \
..
_
-
Solution
Gliadin cD
6.0 P~
...= 58~ Mixing
Q
L4: 5.0 Strength
60 ffiII]
bll
~ 4.0 K·51m
K·l.
Insolubles
Albumins
1.0
Fig. 6. Yields of protein fractions from flours of hard red winter wheat varieties differing in baking quality. C, Comanche; P, Ponca; 58,66-
2558; 60, 66-2560; K-5, K501099; and K-1, K-14042. Mixing strength decreases from left to right. From Huebner and Wall (33).
Drying Air
Temperatura
0::
Nitrogen Extracted
by 0.5% SDS in II 15°C
"' 40
cD
Nitrogen Extracted
by 10% EtOH
pH 10 Borate Buffer
+ II 60°C
0.6% Mercaptoethanol
0::
:a 30
I§) 143°C
...e
z
Nitrogen Extracted
... 20
C;;
c:>
I-
by 0.5% SDS in
pH 10 Borate Buffer
'Q 10
o
Fig. 7. Yields of protein nitrogen extracted by different solvents In sequence from meals of corn dried al different temperatures. From Wall
et al (34).
I \. ,'"
\.\5~ ~\~revor'\
~- ." \ ~\ te, \ . \ . \
\ 0.3 g Alginate
-t--+-'rl-.......,.~b-+-~ nnn- ~ ~ -----\----',----'I---'--\---'c---',----'H-'
\ 33 ml Water \