Food Hydrocolloids 25 (2011) 1853e1864

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Food Hydrocolloids
journal homepage: www.elsevier.com/locate/foodhyd

Food protein functionality: A comprehensive approach

E. Allen Foegeding a, *, Jack P. Davis a, b
a
Department of Food, Bioprocessing and Nutrition Sciences, North Carolina State University, 236 Schaub Hall, Campus Box 7624, Raleigh, NC 27695-7624, USA
b
United States Department of Agriculture, Agricultural Research Service, Market Quality and Handling Research Unit, Raleigh, USA

a r t i c l e i n f o a b s t r a c t

Article history: Food protein functionality has classically been viewed from the perspective of how single molecules or
Received 17 December 2010 protein ingredients function in solutions and form simple colloidal structures. Based on this approach,
Accepted 12 May 2011 tests on protein solutions are used to produce values for solubility, thermal stability, gelation, emulsi-
fying, foaming, fat binding and water binding to name a few. While this approach is beneficial in
Keywords: understanding the properties of specific proteins and ingredients, it is somewhat restricted in predicting
Protein
performance in real foods where the complexities of ingredients and processing operations have
Protein functionality
a significant affect on the colloidal structures and therefore overall properties of the final food product. In
Foams
Gels
addition, focusing on proteins as just biopolymers used to create food structures ignores the biological
Emulsions functions of proteins in the diet. These can be beneficial, as in providing amino acids for protein synthesis
Bioactivity or bioactive peptides, or these can be detrimental, as in causing a food allergic response. This review will
Allergenicity focus on integrating the colloidal/polymer and biological aspects of protein functionality. This will be
done using foams and gels to illustrate colloidal/polymer aspects and bioactive peptides and allergenicity
to demonstrate biological function.
Ó 2011 Elsevier Ltd. All rights reserved.

1. Introduction
Proteins may serve several non-nutritional purposes in foods
but the most common function is to provide and/or stabilize the
characteristic structure of individual foods. For example, in cuts of
meats such as steak that are a portion of a muscle or group of
muscles, the “food structure” is the arrangement of protein-con-
taining connective tissues and myofibrils in muscle fibers that
nature designed to perform the biological function of contraction.
However, in the context of food, this structure also determines in
great part the texture of the cooked meat. Much of meat cookery is
designed to convert the biological structure into a final product that
has the desired textural characteristics. In contrast, milk contains
caseins and whey proteins that exist as a colloidal dispersion and
food processing operations are used to convert the fluid sol into
semi-solid and soft-solid colloidal structures. Processing steps that
concentrate the proteins and favor intermolecular interactions are
essential to the manufacturing of products like cheese and yogurt.
In the biological structure of meat, and the colloidal structure of
cheese, proteins serve as the primary building blocks. Proteins are
also used to stabilize structures in foods, such as emulsions and
foams. The ability to form and/or stabilize networks (gels and
* Corresponding author. Tel.: þ1 919 513 2244; fax: þ1 919 513 8023.
E-mail address: allen_foegeding@ncsu.edu (E.A. Foegeding).
films), foams, emulsions and sols are the main classically viewed
“functional properties” of protein. What is usually minimally
addressed is how these structures alter nutritional properties and
biological activity of proteins. Indeed, a 1981 book entitled Protein
Functionality in Foods (Cherry, 1981) has 14 chapters, 11 of which
cover the classical physical/chemical properties associated with
colloidal system; however, one chapter did address nutrient
bioavailability. The general contribution of proteins/peptides to
nutrition and health, including specific bioactivities, is of increasing
importance prompting development of food products based on
protein-related health issues (Kitts & Weiler, 2003; Norton &
Norton, 2010). Therefore, attention should be given to maintain-
ing nutritional/bioactive properties of proteins when they are being
used to generate food structures. In addition, it is important to be
comprehensive and address some of the undesirable aspects
associated with proteins in foods. Proteins have the ability to bind
flavors and adjustments are often required to assure a desired fla-
vor delivery (Guichard, 2006; Kühn, Considine, & Singh, 2008;
Tavel, Andriot, Moreau, & Guichard, 2008). The main health
concern is allergenic reactions of food proteins. The so-called big
eight foods associated with allergenic reactions are: eggs, fish,
shellfish, milk, peanuts, soy, tree nuts and wheat.
From the previous discussion it would seem that a true defini-
tion of food protein functionality has to cover a range of concerns.
First, a protein has to perform the structural role which is normally
associated with some aspect of colloidal or polymer chemistry.

0268-005X/$ e see front matter Ó 2011 Elsevier Ltd. All rights reserved.
doi:10.1016/j.foodhyd.2011.05.008
1854 E.A. Foegeding, J.P. Davis / Food Hydrocolloids 25 (2011) 1853e1864
Second, it should not diminish another aspect of quality such as
appearance or flavor. Finally, it should provide the desirable food
quality while at the same time delivering the maximum impact on
nutrition and health. In honor of 25 years of Food Hydrocolloids, it
only seems fit to start with an assessment of the number of articles
published in Food Hydrocolloids covering protein functionality.
A key word search of the journal in fall of 2010 turned up the
following number of articles for each of the following: protein
emulsions e 1394; protein gels e 933; protein functionality e 690
and protein foams e 397. The most cited class of proteins for all
categories was whey proteins. It can be seen from the publications
in Food Hydrocolloids alone that this is an expansive subject that is
far beyond the scope of this review. The literature contains exten-
sive reviews on functions of specific protein such as egg (Mine,
1995) wheat (Veraverbeke & Delcour, 2002), sunflower
(González-Pérez & Vereijken, 2007), milk (Chobert, 2003; de Wit,
1998) and oilseed (Moure, Sineiro, Domínguez, & Parajó, 2006)
proteins, just to name a few. Therefore, this review will focus on the
breadth of the subject and acknowledge that specific aspects of
protein functionality are better covered in more focused reviews.
We will initially address some general considerations in protein
functionality and then focus on protein foams and gel to illustrate
colloidal/polymer aspects of protein functionality. The second
section will cover bioactive peptides and allergenicity regarding
biological function. Finally, a concluding section will discuss inter-
actions among colloidal and biological properties.
2. General aspects of protein functionality
Defining and measuring protein functionality starts at the level
of protein structure. Biological structuralefunctional relationships
are often revealed when the three-dimensional structure of
a protein is determined but that is seldom the complete picture in
food protein functionality because food applications are usually
associated with structural transitions (unfolding in solution or at an
interface) rather than the native structure. A simple model for
protein denaturation is:
N%I/D
Where a native (N) structure is reversibly converted to an
intermediate (I) state where tertiary structure is changed but much
of the secondary structure remains, and further unfolding produces
a denatured (D) state. While the three-dimensional native struc-
tures of many food proteins are known, the fine structure of
denatured proteins is much less understood. If one assumes that
denaturation is the opposite of protein folding, then structures
associated with the folding pathway can be used to represent
denaturation (Fig. 1). The validity of this approach is supported by
nuclear magnetic resonance studies of heat denaturation (Belloque
Fig. 1. Folding pathway for b-lactoglobulin. Reprinted with permission from Macmillan Publishers Ltd: Nature Structural Biology Kuwata et al. (2001).
& Smith, 1998; Edwards, Jameson, Palmano, & Creamer, 2002) and
folding (Kuwata et al., 2001; Sakurai, Konuma, Yagi, & Goto, 2009)
of b-lactoglobulin both indicating that b-strands F, G and H are the
most stable (last denatured and first folded) elements of the
structure. There are various molecular properties associated with
each state that have an impact on functional properties (Table 1).
Molecular weight and primary structure will not be changed during
the denaturation process and are considered constants. The
isoelectric point can vary due to intermediate and denatured
(unfolded) structures exposing charged amino acids to new local
environments. The main changes are in secondary and tertiary
structure that can alter the surface exposure of amino acids. This
cumulates in an increase in interaction potential, favoring aggre-
gation, and the loss of structural epitopes for allergenicity. There-
fore, determining the specific structural transitions during folding/
unfolding for food proteins is essential to understanding of the
molecular basis of functionality.
There is a general tendency in the food science literature to
report simple quantitative measurements of food protein func-
tional properties. This is especially seen in protein ingredients
where a numerical rating is desired to determine if that ingredient
will provide a specific function in a formulation. Ideally, there
would be a series of tests that measures each “functionality” and
the resulting numerical ratings could be used by product devel-
opers in making ingredient choices. For example, if you wanted to
make a protein foam, you could pick a protein with scores for foam
generation of “X” and stabilization of “Y” or higher. This approach
has two major assumptions: 1) the foaming test used is robust
enough to be applicable to all foams and 2) that other components
in the food do not alter foaming properties. These assumptions are
clearly flawed and explain why simple tests on protein ingredients
often fail to predict performance in a food. The difficulty in directly
measuring structural properties associated with food functionality
is reflected in methods used to determine functionality. A book
titled “Methods of Testing Protein Functionality” describes tests for:
solubility, viscosity, gelation, foaming, emulsification, water and fat
holding and surface hydrophobicity (Hall, 1996). As can be seen,
some of these methods measure molecular properties (e.g.,
viscosity and surface hydrophobicity); others require forming
a colloidal dispersion (e.g., foam or emulsion); while still others
involve properties of powders (e.g., solubility and some water
binding or sorption methods). A general model for constructing
a protein-based food is shown in Fig. 2. Overlaying functionality
tests on the model shows that typical functionality tests cover the
basic operations of forming a protein dispersion and transforming
it to a colloidal structure; however, these tests seldom account for
addition of non-protein solutes and all of the processing operations
involved in making a food product. The biggest gap is in deter-
mining how proteins function in transforming the food colloidal
structure into a food product. Typical unit operations involve
 E.A. Foegeding, J.P. Davis / Food Hydrocolloids 25 (2011) 1853e1864 1855

Table 1
Molecular properties associated with native (N), intermediate (I) and denatured (D) structures of proteins.

Properties of native Key factors Change in N / I Change in I / D

state
Molecular weight Determines general polymer properties No No
Isoelectric point Determines phase stability Possible due to altered Possible due to altered
pKas of functional groups pKas of functional groups
Primary structure Sequence of non-polar, polar and No No
charged amino acids
Sequential epitopes No No
Bioactive peptides No No
Secondary structure Amount of a-helix, b-sheets and Very little Yes
other structures
Tertiary structure Overall structure Yes Yes
Structural epitopes Yes Yes
Surface topology Groupings of non-polar, polar and charged Yes Yes
amino acids in surface-assessable space

heating and mass transfer (e.g., evaporation of water) to set-up the
final food structure.
2.1. Modification to improve functionality
One goal of understanding molecular mechanisms for protein
functionality is to provide a directed, and logical, structural-based
approach to alter functionality. As seen in an early investigation
on modifying whey proteins to foam like egg albumin, “The
possession of these characteristics (in regards to foaming properties)
in a much lower-priced product (i.e., whey proteins). would result,
therefore, in its extended use” (Peter & Bell, 1930). While finding
low cost alternatives is still a viable motivation, the ability to select
among proteins for health and safety reasons is another consider-
ation. Protein functionality is often associated with changes in
secondary and tertiary structure (heat denaturation for gelation;
unfolding at an interface), so treatments such as high pressure have
been used to alter structure and functional properties (Galazka,
Dickinson, & Ledward, 2000; López-Fandiño, 2006). The amino
acid lysine contains an e-amino group that contributes to the net
charge and nucleophilic properties allows for reactions with
carbonyl compounds found in foods. The most exploited approach
is to use the start of the Maillard reaction to either: 1) modify
protein charge and/or 2) attach a sugar or oligosaccharide and form
a conjugated molecule (Campbell, Raikos, & Euston, 2003; Oliver,
Melton, & Stanley, 2006) which in turn affects functionality.
Protein charge and isoelectric point can also be altered by deami-
dation (Hamada, 1994; Wright, 1991). Another approach is to form
covalent links between proteins by enzymatic or chemical reactions
making polymers of individual or a mixture of proteins (Buchert
et al., 2010). This can be used to make modified ingredients or in
combination with forming specific structure (e.g., adding cross-
links in gels). An opposite approach is to enzymatically hydrolyze
the protein to varying degrees (Kilara & Panyan, 2003; Kristinsson &
Rasco, 2000). In these and other modifications, the significance of
the modification is usually based on how it alters the results of

Fig. 2. Processes involved in manufacturing a food with protein-based colloidal structures. Proteins are formed into dispersions that are converted to colloidal structures. The
colloidal structures undergo a final transformation (which may or may not involve thermal processing) into a food product. Functional properties and effects on allergenicity and
bioactivity are listed under appropriate headings.
1856 E.A. Foegeding, J.P. Davis / Food Hydrocolloids 25 (2011) 1853e1864
specific tests for protein functionality. As discussed later, all func-
tionality modifications mentioned, i.e., Maillard type reactions to
form protein/sugar adjuncts, deamidation, enzymatic crosslinking
or enzymatic hydrolysis, also have the potential to directly impact
the allergenicity and/or bioactivity of the modified protein source.
2.2. Protein functionality in food systems
The simplest approach to understanding protein functionality is
to examine single protein solutions/dispersions. For example,
b-lactoglobulin is one of the most studied food proteins regarding
functionality and a recent review presents a comprehensive model
for denaturation and aggregation at temperatures ranging from 20
to 150  C (de Wit, 2009). However, protein ingredients are generally
a mixture of proteins (e.g., whey or egg white proteins) and other
molecules such as sugars and minerals. Hence, when a protein
ingredient is added to a formula it is often adding more than just
protein. Moreover, protein ingredients are one of several ingredi-
ents in foods and therefore must “function” in a complex system.
Therefore, protein functionality will be discussed in the context of
providing an overall food structure rather than just one aspect of
the overall structure (e.g., surface activity).
3. Foams
Foams are defined as gas in liquid (G/L) dispersions or gas in
solid (G/S) materials. Foam structures are components of many
foods such as meringue (G/L) and bread (G/S). In its simplest form,
a foam consists of a dispersed gas bubble surrounded by a contin-
uous phase (Campbell & Mougeot, 1999). Proteins are located in the
continuous phase and at the interface. Proteins are generally
distinguished from small molecular weight surfactants in that they
have the ability to interact with adjacently adsorbed proteins to
form interfacial films that have properties of: thickness, gas
permeability, shear viscoelasticity and dilatational viscoelasticity
(Dickinson, 1992, 1999; Wilde, Mackie, Husband, Gunning, &
Morris, 2004). Therefore, one functional property of proteins in
foams is the ability to form interfacial films with varying degrees of
the aforementioned physical properties. Interfacial films tend to be
investigated under two concentration regimes. In dilute solutions,
the majority of the protein is at the interface with a minimal
concentration remaining in the continuous phase. This tends to be
in the micromolar or lower protein concentration range (Cornec,
Cho, & Narsimhan, 1999; Paulsson & Dejmek, 1992; Wierenga,
van Norél, & Basheva, 2009). In contrast, food foams are generally
formed under millimolar protein concentrations where there is an
excess amount of protein in the continuous phase, presenting the
possibility of exchange with the interface (Nicorescu et al., 2011;
Yang & Foegeding, 2010). This additional dynamic is minimal in
dilute solution studies and should be considered as a potential
contribution as to how proteins function in food.
Foams are considered “bubbly” if the gas phase volume is below
a close packing level and “polyhedral” if above (Dickinson, 1992).
The polyhedral packing arrangement forms Plateau borders among
three adjacent bubbles. The film separating the bubbles will drain
into the Plateau border because the Laplace pressure inside the
Plateau border is lower than that of the adjacent films (Walstra,
2003). Proteins can function in the continuous phases of bubbly
and polyhedral foams by contributing to the viscosity or by possibly
forming a network. The latter is seen in marshmallows where
a gelatin gel is formed around entrapped bubbles. Food products
are often wet foams turned into dry foam (Campbell & Mougeot,
1999). For example, meringues and bread dough start as a wet
foams but require drying to set into the final structures. Therefore,
the structural responses of proteins during heating and drying are
also key to functionality. This is apparent when a whey protein
foam is substituted for an egg white foam in making angel food
cake (Foegeding, Luck, & Davis, 2006). The wet foams have similar
properties, but the two protein sources do not have the same ability
to stabilize the foam during the baking process (Berry, Yang, &
Foegeding, 2009; Pernell, Luck, Foegeding, & Daubert, 2002).
3.1. Protein functionality in foams
The ability of individual proteins to form interfacial films and
foams is beyond the scope of this review but a few points are worth
noting. In milk proteins, the intrinsically unfolded structure of
caseins, in contrast to the compact globular structure of whey
proteins, alters their film forming ability and thereby foaming
properties (Marinova et al., 2009; Williams & Prins, 1996). There is
also the possibility of finding protein in nature with novel func-
tionality. Such is the case with hydrophobins, which show excep-
tionable ability in stabilizing foams (Cox, Aldred & Russsell, 2009;
Tchuenbou-Magaia, Norton, & Cox, 2009).
Foods that contain foam structures must be considered in the
context of three important and partially distinct stages: formation,
stability and consumption. In foam formation, proteins contribute
by rapidly adsorbing at freshly formed air/water interfaces during
which interfacial tension is lowered, and by altering the viscosity of
the continuous phase. Once formed, proteins can contribute to the
prevention of the following foam destabilization mechanisms by
several means (Damodaran, 2005; Dickinson, 1992; Hilgenfeldt,
Koehler, & Stone, 2001; Koehler, Hilgenfeldt, & Stone, 2000;
Martin, Grolle, Bos, Stuart, & van Vliet, 2002; Murray, 2007;
Rodríguez-Patino, Sanchez, & Nino, 2008; Wilde, 2000):
Creaming e As formally described by Stokes Law, the rise of gas
bubbles is very rapid because of the large density difference
between the continuous phase and gas and the tendency of bubbles
to be large (both of these factors are evident when comparing with
emulsions; for example see Table 11.1 in Walstra (2003)). Proteins
tend to contribute less to the viscosity of the continuous phase and
provide the most resistance to creaming by forming a network to
immobilize gas bubbles. This is seen in marshmallows and gelatin
desserts containing gas bubbles.
Flocculation e Surface interactions among bubbles without film
rupture and coalescence depends on the disjoining pressure
(Stubenrauch & von Klitzing, 2003) between droplets and this can
be influenced by interfacial protein films.
Coalescence e The joining of two gas bubbles into one requires
drainage of the continuous phase between two bubble surfaces
coupled with rupture of the protein interfacial film. The ability of
proteins to form strong, elastic films at the interface resists rupture.
Disproportionation e The movement of gas from small to large
bubbles can be restricted by forming a protein film that is resistant
to shrinkage and one that has low gas permeability. This again gets
back to the type of film that is created and how its properties are
altered by other ingredients.
3.2. Altering foaming functionality
An ever-present goal is to modify proteins to improve func-
tionality. This takes on a variety of molecular approaches (as dis-
cussed in Section 2.1) but the final determination of effectiveness is
demonstrated improvement in foam formation, stability or moving
to a desirable level of a physical property such as foam yield stress.
One of the simplest ways to alter functionality is by mild heat
treatments that alter protein structure and cause aggregation but
do not result in large scale protein precipitation. This has been
shown to improve the formation (so-called foamability) and
stability of whey protein and egg white foams (Davis & Foegeding,
 E.A. Foegeding, J.P. Davis / Food Hydrocolloids 25 (2011) 1853e1864
2004; Nicorescu et al., 2009; Moro, Báez, Busti, Ballerini, &
Delorenzi, 2011). Complexing proteins with polysaccharides can
be associated with increased or decreased stability (Dickinson,
2003). Since foam stability is greatly dependent on properties of
the interfacial film, ingredients that alter film composition and
characteristics will affect the overall functional outcome. This is
very apparent when small molecular weight surfactants are mixed
with proteins in foaming applications which can result in foam
destabilization (Coke, Wilde, Russell, & Clark, 1990; Horne,
Atkinson, Dickinson, Pinfield, & Richardson, 1998; Mackie,
Gunning, Wilde, & Morris, 1999; Morris & Gunning, 2008).
Particle-based stabilization offers the possibility of long-term foam
stability (Alargova, Warhadpande, Paunov, & Velev, 2004; Binks,
2002; Du et al., 2003). A novel approach of using surface food
grade particles and proteins has been shown to improve bubble
stability by a proposed “increased jamming of particles at the
interface” (Murray, Durga, Yusoff, & Stoyanov, 2011). One last point
to consider is the possibility of anti-foaming agents in a food
system. These could be an inherent component of protein ingre-
dients or part of the food formulation. Oil-based anti-foams are
used for many industrial applications and the mechanism of foam
destruction by oils should be considered when evaluating foaming
of ingredients and foods (Denkov, 2004).
4. Gels
Protein sols are converted to gels by a range of processes that
increase intermolecular interactions. The prominent covalent
interaction is disulfide bonds but iso-amide bonds can also be
created by using the enzyme transglutaminase. Non-covalent
interactions (hydrogen bonding, hydrophobic interactions and
electrostatic interactions) are present in varying degrees and it is
the mixture of covalent and non-covalent interactions that makes
modeling protein gelation challenging and at the same time
provides for a range of textural properties (i.e., protein function-
ality). Once the degree of intermolecular linking reaches to a point
where a continuous network is formed, the macroscopic property
of elasticity is developed and the system is considered a gel. Protein
functionality regarding gelation can be separated into factors
determining gel formation and the physical properties of the gel.
The basic requirement for gelation functionality in a particular food
is formation of a network under the constraints of food composi-
tion and manufacturing. The basic mechanism(s) of protein gela-
tion (i.e., converting a fluid into a solid by forming
a macromolecular network) has received considerable attention
(for example, Clark, Kavanagh, & Ross-Murphy, 2001; Clark & Ross-
Murphy, 1987; van der Linden & Foegeding, 2009; Nicolai & Durand,
2007) and will not be addressed in this review. Macroscopic
properties, such as moisture/fat release and sensory texture, are
due to gel network structure and interactions linking proteins and
other macromolecules in the network. This is reflected in the
measurement of fat and water holding as functional properties of
proteins (Barbut, 1996). Protein gel structure is also responsible for
the breakdown pattern that is perceived as food texture. For
example, hardness, perceived as the biting force required to cause
fracture, is a common sensory attribute of foods with gel structures
such as cheese, gelatin desserts, tofu and processed meats. Protein
functionality for gelation is therefore: a) conditions for gelation
including critical protein concentration and factors increasing
intermolecular interactions; b) interactions with other components
such as polymers above or below the binodal; and c) proteine-
protein interactions leading to a micro-phase separated or single
phase system. These will depend on protein size, shape, isoelectric
point, types of intermolecular interactions and structural
1857
distribution of charged, hydrophobic and other amino acids, as well
as solvent conditions.
4.1. Protein functionality in regards to gel structure
Food protein gels can be separated based on physical and
sensory properties into semi-solids (e.g., yogurt) and soft-solids
(e.g., cheddar cheese). The types of structures observed will vary
with protein type and gelation conditions but can roughly be
considered as a primary aggregate (aggregates of several proteins
that remain dispersed and have a characteristic shape such as
flexible strand, rigid rod or globular) that undergoes secondary
aggregation to form a gel network (van der Linden & Foegeding,
2009). Two factors that always need to be considered in evalu-
ating protein functionality are electrostatic conditions (pH and salt
concentration) and protein concentration. The seminal work of
Clark, Tuffnell, Saunderson, Suggett, Judge and Stubbs established
how pH and ionic strength contributed to network structure and
what was subsequently termed particulate and fine-stranded gel
networks (Clark & Tuffnell, 1980; Clark, Judge, Richards, Stubbs, &
Suggett, 1981; Clark, Saunderson, & Suggett, 1981). Fine-stranded
gels form when electrostatic repulsion is favored among mole-
cules and the structures formed under these conditions have
recently been reviewed (van der Linden & Venema, 2007). Partic-
ulate structures are formed where there is minimal net charge on
proteins (at and near the isoelectric point) or where there is
extensive charge screening due to a high concentration of ions in
solution. This gel structure is noted for having low water-binding
capacity due to the gel network containing large pores (Barbut,
1995). Forming roughly spherical particles (i.e., primary aggre-
gates) under these conditions has been shown to be a general
property for a range of proteins; with particle diameters varying
due to heating rate and specific protein (Bromley, Krebs, & Donald,
2006; Krebs, Devlin, & Donald, 2007). The shift between solution
conditions that favor fine-stranded and particulate gels
was recently described based on protein phase stability. Ako,
Nicolai, Durand, and Brontons (2009) proposed that protein
concentration and pH/salt effects on heat denaturation/aggregation
of b-lactoglobulin can be explained based on the protein being in
single-phase or micro-phase separated regions. The micro-phase
separated region would be defined, in the absence of added salts,
as the pH region around the isoelectric point where micro-phase
separation occurs (4.1e5.6 for b-lactoglobulin with an isoelectric
point of 5.2). At pH values outside of this region, homogeneous or
micro-phase separated regions depend on salt and protein
Fig. 3. State diagram for a pH 7 b-lactoglobulin solution after heating. Solution or gel
states are shown as a function of salt (Cs) and protein (C) concentration. Reprinted with
permission from Ako, Nicolai, Durand, and Brotons (2009).
1858 E.A. Foegeding, J.P. Davis / Food Hydrocolloids 25 (2011) 1853e1864
concentration. As shown in Fig. 3, a 40 g/L b-lactoglobulin solution
at pH 7 will progressively form a sol, homogeneous gel, micro-
phase separated gel and precipitate coinciding with an increase
in salt concentration. This general behavior was previously noted
with a range of proteins based on analyzing the dry matter content
of aggregates (Hegg, 1982). An additional approach to generate
different protein gel structures is to pre-form primary aggregates
and then combine them into a gel network (Donato, Kolodziejcjk, &
Rouvet, 2011; Vardhanabhuti, Foegeding, McGuffey, Daubert, &
Swaisgood, 2001). This provides a way to alter gel network prop-
erties under fixed solution conditions (pH and ionic strength).
4.2. Modification of function based on other molecules
If the focus on protein functionality is to generate gel structures
with a range of textural and water-holding properties, then one of
the easiest ways to alter structure is by interactions with other
polymers. The use of proteinepolysaccharide mixtures to change
food properties has received considerable attention (for example,
see reviews of Dickinson, 1998; Kasapis, 2008; Ledward, 1993;
Turgeon, Beaulieu, Schmitt, & Sanchez, 2003) so just a few points
concerning gel structure will be addressed. Conditions that
promote segregative phase separation can increase or decrease gel
firmness (G0 ) depending on polymer concentration and solution
conditions (Bertrand & Turgeon, 2007; Fitzsimons, Mulvihill, &
Morris, 2008). Proteinepolysaccharide mixtures can also be used
to alter fluid released from gels, thereby changing the “watery”
perception during chewing (van den Berg, van Vliet, van der Linden,
van Boekell, & van de Velde, 2007). In addition, the sensory
perception of crumbliness can be adjusted with proteine
polysaccharide mixtures (van den Berg et al., 2008). The type of
microstructures generated depend on the protein aggregation
process and polysaccharide properties; so, protein functionality in
this situation is partially associated with factors determining
protein aggregation (Baussay, Durand, & Nicolai, 2006; Baussay,
Nicolai, & Durand, 2006; de Jong, Jan Klok, & van de Velde, 2009).
5. Protein/peptide allergenicity/bioactivity e general
Work to understand the allergenic and bioactive properties of
food proteins and peptides are two highly active areas of research.
Allergenic and bioactive properties of proteins/peptides are clearly
different. Food allergies are adverse immunological responses to
proteins/peptides, whereas bioactivities are health benefits gained
from protein/peptide consumption that extend beyond amino acid
incorporation as necessary for adequate human health. Despite this
obvious difference, factors that determine the potential of food
proteins/peptides to be either allergenic or bioactive share many
important similarities as discussed subsequently and as summa-
rized in Table 2. Essentially all proteins, and peptides of a minimum
length, have inherent allergenic and bioactive potentials which are
largely defined by the primary sequence of amino acids (Table 1).
However, any process utilized to improve food quality that modifies
protein/peptide structures can largely enhance or decrease these
potentials (Fig. 1, Table 1).
In the case of food allergies, most research focuses on intact
proteins, but a primary consideration is how these proteins, as
Table 2
Comparison of bioactive and allergenic proteins/peptides.
Biological effect Protein
sources
Bioactive Positive All
Allergenic Negative All
components within complex food matrices, are digested into
peptides. In the case of bioactive properties, most literature focuses
on peptides. The release of bioactive peptides may occur after
gastrointestinal fluids act on the intact proteins, or the peptides
may be generated from the parent proteins during food processing
and then consumed (Kitts & Weiler, 2003). In the latter case, such
peptides still must be considered in the context of the gastroin-
testinal tract and effects of this environment on further peptide
breakdown and subsequent uptake. The digestion process ulti-
mately results in peptides having the capacity to 1) negatively
interact with immune system in the case of allergies or 2) positively
interact with human body in the case of bioactivities. A compre-
hensive review of food protein/peptide allergenicity and bioactivity
is not practical nor the goal of this section; instead common factors
contributing to the potential of food proteins/peptides to be aller-
genic and/or bioactive will be discussed. Emphasis will be given to
some key food processes designed to improve protein functionality
and hence food quality, and how these processes can affect protein/
peptide allergenicity or bioactivity either positively or negatively.
While allergic reactions are possible to protein from any food,
the majority of cases are attributed to proteins from: eggs, fish,
shellfish, milk, peanuts, soy, tree nuts or wheat. Interestingly, and
as discussed in more detail later, all of these protein sources are also
well documented sources of bioactive peptides. Most food allergies
are mediated by IgE antibodies with symptoms ranging from
relatively mild, i.e., rash formation or upset stomach, to the most
extreme reaction, anaphylactic shock, which is rare but can be fatal
if not treated properly. Symptom severity depends on a range of
factors including allergic/medical history of the patient, amount of
allergic food consumed, patient age, etc. Excellent reviews are
available describing current understandings for the mechanisms
responsible for the pathogenesis of food allergy, including potential
routes for sensitization in affected individuals (Burks, 2008;
Sicherer & Sampson, 2010). In the U.S., food allergies are reported
to affect approximately 3.9% of children younger than 18 years, with
an approximate 18% increase in reported food allergy from 1997 to
2007 (Branum & Lukacs, 2009). Numerous other studies report food
allergy to be on the rise, especially in Westernized countries.
Multiple factors are hypothesized as contributing to this increase,
including the “hygiene hypothesis”, changing patterns in food
introduction for infants, heightened awareness of the disorder, and
changes in the modern diet (Sampson, 2004; Sicherer & Sampson,
2007). Regardless of the reasons, it is clear that food allergies are
affecting large segments of the population. As such, it is imperative
for food scientists working with proteins to not only consider food
protein functionality, but also protein allergenicity.
Bioactive proteins/peptides induce positive biological effects
when absorbed by the human body. These positive biological
effects or “bioactivities” are outside the realm of classical protein
nutrition considerations, i.e., adequate protein/amino acid intake
for muscle development. Instead, these bioactivities approach
medicinal qualities with descriptions of antihypertensive, immu-
nomodulatory, anti-inflammatory, antioxidant and hypocholester-
olemic effects being common (Kitts & Weiler, 2003; Korhonen &
Pihlanto, 2003; Megias et al., 2004). Proteins/peptides can also
have important bioactivities in foods prior to consumption. As an
example, nisin is a natural antimicrobial peptide industrially
Minimal peptide Importance of conformation Digestive Food matrix
length effects effects
2e10 Yes e less documented Yes Yes
5e8 Yes Yes Yes
 E.A. Foegeding, J.P. Davis / Food Hydrocolloids 25 (2011) 1853e1864
produced by diary fermentation using strains of Lactococcus lactis
subsp. lactis coupled with downstream purification, and this 34
amino acid polypeptide is widely used as an antimicrobial agent in
various cheeses (de Arauz, Jozala, Mazzola, & Penna, 2009). Lacto-
ferrin is an iron binding glycoprotein found in milk that has gained
significant interest for its bioactivity, both as an antimicrobial agent
in foods, but also as a source of peptides with a multitude of
described bioactivities (Wakabayashi, Yamauchi, & Takase, 2006). It
should also be noted that lactoferrin is an established milk allergen.
5.1. Allergenicity/bioactivity e structural considerations
The linear sequence of amino acids within a given protein/
peptide is a primary contributor to its potential to be either aller-
genic and/or bioactive. Although the exact mechanisms responsible
for food allergy are not completely understood, it does appear that
most food allergenic proteins bind IgE and cause crosslinking on
the surface of mast cells which results in downstream cascades
leading to the allergic response (Burks, 2008; Sicherer & Sampson,
2010). Portions of a protein that bind IgE are referred to as epitopes.
Epitopes are attributed to either a given linear sequence of amino
acids within the protein, or to a portion of the three-dimensional
structure of the protein, and are designated as either linear or
conformational, respectively. Analogous to linear epitopes with
regards to allergenicity, the bioactivity of given peptides are largely
attributed to linear sequence of amino acids. Generally speaking,
such bioactivities result from interactions between “active”
sequences of peptides and the multitudes of biological molecules
found throughout the human body, including the various cell
receptors, enzymes, etc. responsible for human wellbeing. With
this general definition in mind, all food proteins are thought to
contain bioactive peptides. As mentioned previously, some of the
best studied and documented sources of bioactive peptides include
the “big eight” allergens, i.e., eggs (Mine, 2007), fish (Vercruysse,
Van Camp, & Smagghe, 2005), shellfish (Cudennec, Ravallec-Ple,
Courois, & Fouchereau-Peron, 2008), milk (Kamau, Cheison, Chen,
Liu, & Lu, 2010; Pihlanto, 2006), peanuts (Quist, Phillips, & Saalia,
2009), soy (Wang & De Mejia, 2005), tree nuts (Martinez,
Labuckas, Lamarque, & Maestri, 2010) and wheat (Zhu, Zhou, &
Qian, 2006), with those of milk, eggs and soy being the best char-
acterized. A likely reason why these proteins are such well known
sources of bioactive peptides is that each of these proteins derives
from primary sources of food worldwide.
The majority of epitopes from allergic proteins are thought to be
at least 8 amino acids long; however, sequences as short as 5 amino
acids have been identified as epitopes (Bannon & Ogawa, 2006).
Various bioinformatic approaches are being utilized to predict
potential allergenicity of novel food proteins by cross referencing
sequence data to known allergens (Bannon & Ogawa, 2006;
Ivanciuc et al., 2009). However, across all documented food aller-
gens, no obvious commonalities seem to exist for linear epitopes.
The majority of food bioactive peptides are 2e10 amino acids long,
although much longer bioactive sequences having been described
(Kitts & Weiler, 2003). Bioinformatic approaches to identifying food
bioactive peptides are also becoming more prevalent (Majumder &
Wu, 2010; Minkiewicz, Dziuba, Darewicz et al., 2008; Minkiewicz,
Dziuba, Iwaniak, Dziuba, & Darewicz, 2008), but again no obvious
commonality is known to exist for all bioactive peptides which
could be attributed to the wide range of bioactivities having been
described and yet to be discovered. Linear allergenic epitopes can
be mapped using overlapping synthetic peptides, a strategy utilized
to characterize the linear epitopes of the predominant peanut
allergens, Ara h 1e3 (Burks et al., 1997; Rabjohn et al., 1999; Stanley
et al., 1997). In the case of bioactive peptides, various chromatog-
raphy based strategies, often coupled with Edman sequencing, have
1859
been employed to determine peptide sequence (Wang & De Mejia,
2005). Advanced LCeMS techniques are also becoming more
common for determining bioactive peptide sequences (Wang & De
Mejia, 2005).
Beyond linear epitopes, the three-dimensional structures of
proteins/peptides play significant roles in determining allergenicity.
Conformational epitopes are portions of a protein defined by a three-
dimensional space that react with IgE resulting in an allergenic
reaction. While the tendency seems to be to define epitopes as either
linear or conformational, the reality is likely that the reactivity of
most epitopes is a combination of both (Bannon & Ogawa, 2006). All
peptides have elements of three-dimensional structures that
become more important at longer chain lengths. While the primary
sequence of amino acids is an important contributor to the 3-D
confirmation adopted by a protein/peptide, work has shown that
proteins with vastly different primary sequences can form similar
3-D arrangements. Alternatively, proteins with highly homologous
sequences can adopt quite different 3-D folds (Alexander, He, Chen,
Orban, & Bryan, 2007). As such, conformational epitopes are gener-
ally more difficult to define and knowledge of conformational
epitopes has generally lagged that of linear epitopes (Bannon &
Ogawa, 2006). In the case of specific food bioactive peptides, many
active sequences have been defined at the sequence level; however,
conformational domains within proteins/peptides, while less docu-
mented, have been shown to influence bioactivities. For example,
various confirmers of a 5 amino acid peptide synthesized in different
fashions had significantly different inhibitory potentials against
Angiotensin-I-converting enzyme (ACE) due to different 3-D
confirmations (Gomez-Ruiz, Recio, & Belloque, 2004).
5.2. Allergenicity/bioactivity e digestion
Protein allergenicity is characterized by the presence of epitopes
and the availability of these epitopes to sensitize, and upon addi-
tional exposure, subsequently react with the immune system of
sensitized individuals. While some exposure/adsorption is expec-
ted in the mouth, the majority of allergen interaction with the body
occurs at the lumen of the GI tract (Sicherer & Sampson, 2010). As
such, the capacity of a protein to resist the acidic and proteolytic
environment of the stomach is thought to contribute to a protein’s
allergic potential, although such resistance is not necessarily
a prerequisite for allergenicity (Fu, Abbott, & Hatzos, 2002). Resis-
tance to simulated digestive fluid is one of many tools utilized to
assess potential allergenicity of novel proteins such as those found
in genetically engineered crops (Thomas et al., 2009). Multiple
in vitro models of digestion, with varying degrees of complexity,
have been described in the scientific literature in the context of
protein allergenicity (Moreno, 2007). Issues surrounding the
development, utility and relevance of these models to protein
allergenicity have been reviewed (Moreno, 2007; Thomas et al.,
2009). Protein incorporation into colloidal structures such as gels,
foams or emulsions also affects subsequent protein digestion
(Mackie & Macierzanka, 2010). Protein adsorption at interfaces may
limit exposure of adsorbed portion of the protein to digestive
enzymes, but the general increase in molecular flexibility resulting
from adsorption generally seems to increase proteolysis (Mackie &
Macierzanka, 2010). Along these lines, work is also ongoing to
better understand interactions and influence of biosurfactants
found in digestive fluids on the digestibility of adsorbed proteins.
All previous examples of research involving simulated in vitro
protein digestion pertained to allergenicity; however, the release of
bioactive peptides during digestion and subsequent uptake by the
body makes such models directly relevant to better understanding
protein/peptide bioactivity (Picariello et al., 2010).
1860 E.A. Foegeding, J.P. Davis / Food Hydrocolloids 25 (2011) 1853e1864
5.3. Allergenicity/bioactivity e processing and food matrix effects
While a great deal of relevant research has been conducted
using isolated and/or recombinant food proteins to characterize
structure and other properties relevant to allergenicity, the reality
is that allergenic proteins are typically consumed as a component
within a complex food matrix. Such matrices are extremely variable
and the range of food processes utilized to improve quality of such
food matrices is equally variable. Together, processing and food
matrix effects greatly influence the potential of food allergens to
react with sensitized individuals (Mills & Mackie, 2008; Nowak-
Wegrzyn & Fiocchi, 2009). Sugars, polysaccharides and lipids are
common examples of molecules that can react with proteins,
typically during a processing operation, and affect the allergenic
potential of a protein. For example, phospholipids were shown to
have a protective effect on the allergenicity of a-lactalbumin during
simulated in vitro digestion (Moreno, Mackie, & Mills, 2005). As
another example, pectin gels, under acidic conditions simulating
the gastric environment, protected fruit allergens from pepsin
digestion and subsequent breakdown in simulated intestinal
conditions (Polovic et al., 2009).
Conformational epitopes are generally considered more
susceptible to destruction by processing operations. The classic
example is thermal denaturation of proteins which modifies
structural epitopes to the point of not being able to bind IgE, or the
epitopes are rendered less available during digestion due to protein
aggregation and/or interactions with the surrounding food matrix.
Alternatively, protein modification in a food resulting from heat or
some other input could lead to the formation of neoepitopes with
enhanced reactivity. Recent studies involving cow’s milk, egg and
peanut allergies emphasize the importance of understanding
conformational epitopes and modification of these epitopes in
complex foods. Cow’s milk allergy is the most common childhood
allergy and 68 of 100 children with documented cow’s milk allergy
tolerated extensively heated milk in the form of muffins or waffles
(Nowak-Wegrzyn et al., 2008). Immunological evidence suggests
that patients who tolerated the extensively heated milk proteins
primarily reacted to conformational epitopes, whereas patients
who did not tolerate the extensively heated milk proteins primarily
reacted to sequential or linear epitopes (Nowak-Wegrzyn et al.,
2008). Similarly, the majority of children who outgrow cow’s milk
allergy (80% of patients with this allergy) primarily display IgE
reactivity to conformational epitopes (Chatchatee, Jarvinen,
Bardina, Beyer, & Sampson, 2001).
In the case of egg allergy, a recent study showed that 64 of 91
children tolerated extensively heated egg proteins, again in the
form of muffins or waffles (Lemon-Mule et al., 2008). Immuno-
logical evidence suggested that patients tolerant of extensively
heated egg white were primarily reactive to conformational
epitopes. Ovomucoid, which is a water-soluble glycoprotein with
a MW of w28,000 Da representing roughly 10% of egg white
proteins, is considered the most pathogenic allergen in hen egg
white (Lemon-Mule et al., 2008; Urisu et al., 1997). Ovomucoid is
highly heat stable in model systems with subsequent retention of
allergenic properties (Urisu et al., 1997). In contrast, ovalbumin,
which is another documented allergen in hen egg white and
represents roughly 50% of the protein, is highly heat labile, with
heating typically resulting in loss of allergenic potential (Lemon-
Mule et al., 2008; Tanabe, Tesaki, & Watanabe, 2000). Accord-
ingly, patients tolerant of products containing extensively heated
egg products generally were immunologically less reactive to
ovomucoid as compared to those who did react to the heated egg
white products (Lemon-Mule et al., 2008). Studies with egg white
proteins in model systems have shown ovomucoid forms insol-
uble complexes with gluten resulting in decreased solubility and
decreased allergic potential (Kato, Ozawa, & Matsuda, 2001),
suggesting these reactions are important to subjects with docu-
mented egg white allergy who are able to tolerate extensively
heated egg white in the form of muffins or waffles (Lemon-Mule
et al., 2008). Accordingly, egg white fractions selectively reduced
in ovomucoid are generally better tolerated by allergic individ-
uals as compared to traditional egg white preparations (Urisu
et al., 1997).
Peanut allergy is another common food allergy, estimated to
affect roughly 1% of children in North America and the U.K
(Sicherer & Sampson, 2010). Peanut is considered one of the most
severe food allergies, with the majority of fatal food allergic
reactions reported in the US having resulted from peanuts (Bock,
Munoz-Furlong, & Sampson, 2007). Furthermore, unlike most
food allergies, only about 20% of children allergic to peanuts
outgrow this disorder (Skolnick et al., 2001). The majority of
peanuts in North America are dry roasted, which has been shown
to enhance the IgE binding capacity of peanut proteins as
compared to raw controls. This enhanced binding is attributed to
the enhanced reactivity of protein/sugar adjuncts resulting from
Maillard type reactions during dry roasting (Gruber, Becker, &
Hofmann, 2005; Maleki, Chung, Champagne, & Raufman, 2000;
Maleki et al., 2003). In contrast, boiling of peanuts has been
shown to significantly decrease the IgE binding capacity of peanut
protein (Mondoulet et al., 2005). Protein from boiled peanuts
shows minimal evidence of Maillard reactions presumably due to
the higher moisture content of this product during heating
(Schmitt, Nesbit, Hurlburt, Cheng, & Maleki, 2010). A complicating
factor in studies investigating thermal processing effects on
protein allergenicity is that thermal modifications typically
decrease solubility, which is a prerequisite for many standard
in vitro assays addressing allergenic potential; however, such
insoluble fractions may well be physiologically relevant (Schmitt
et al., 2010). Insoluble fractions from boiled, dry roasted, and oil
roasted peanuts all showed substantial IgE binding when re-
solubilized in a typical SDS PAGE buffer (Schmitt et al., 2010).
Western blots suggested that Ara h 1, a predominant peanut
allergen and w63 kDa glycoprotein, was more involved in the
formation of covalently linked, higher molecular weight
complexes attributed to Maillard reactions as compared to another
predominant peanut allergen, the w19 kDa Ara h 2. These insol-
uble complexes were much more intense in dry roasted and oil
roasted samples as compared to boiled samples (Schmitt et al.,
2010). Disulfide bonds were not involved in these detected
complexes (reducing conditions) but may well be playing a role
under native conditions. In addition to having increased reactivity
in IgE binding assays, these higher MW Maillard induced
complexes can presumably better resist peptic digestion resulting
in increased opportunity for epitopes to react within the GI tract
(Kopper et al., 2005). These studies reinforce the importance of
considering protein solubility when measuring processing induced
modifications related to allergenicity. Such modifications could
result from heat or any other processing input.
Whereas Maillard browning reactions seem to enhance peanut
protein allergenicity, such reactions have also been attributed to
the potential for decreased allergenicity in other proteins. Maillard
modifications to b-lactoglobulin (Taheri-Kafrani et al., 2009) and
a-lactalbumin (Bu, Lu, Zheng, & Luo, 2009) have been shown to
reduce allergic potential for these primary whey proteins, with
glycation essentially being hypothesized to mask epitopes along
the protein. However, Maillard modifications also seem to protect
b-lactoglobulin during simulated gastric digestion which could
promote allergenicity, meaning this effect must be considered
along with the potential positive benefit of glycation minimizing
allergenicity (Corzo-Martinez, Soria, Belloque, Villamiel, & Moreno,
 E.A. Foegeding, J.P. Davis / Food Hydrocolloids 25 (2011) 1853e1864
2010). Maillard modifications have also been recently shown to
potentially decrease the allergenicity of soy (de Lagemaat, Silvan,
Moreno, Olano, & del Castillo, 2007) and buckwheat (Nakamura
et al., 2008) proteins.
6. Integrating colloidal/polymer properties
and biological activity
Protein functionality was historically a molecularly focused
concept. Each protein molecule or protein ingredients was viewed
as having inherent “gelling, foaming and emulsifying” properties
that could be measured in simple tests. While this is partially true,
it ignores the need to function in the presence of a range of other
molecules and the overall complexity of most foods. A more recent
approach focuses on colloidal and soft matter concepts used to
generate “food structures” with specific properties that elicit
desirable sensory responses and are designed to deliver health and
nutrition benefits (Norton & Norton, 2010; van der Sman & van der
Goot, 2009). One of the key elements of this approach is viewing
a system across length scales (Ubbink, Burbidge, & Mezzenga,
2008). Then the challenge becomes how food proteins (nano
scale) contribute to structures seen at the micro scale (e.g., foam
structure) and how the entire system combines to deliver macro-
scopic properties of foods. This approach has several challenges and
opportunities. The first challenge is to determine how specific
elements of food structure deliver desirable traits such as texture.
As pointed out by Hutchings and Lillford (1988), one element of
texture is the perception of how structure is broken down during
mastication. This implies the need to build structures with specific
breakdown patterns. Once the links between food structure and
sensory enjoyment are established, it is conceivable that a desired
structure can be created by a range of molecules and processes. This
will allow for manipulation of composition, say based on health
concerns such as allergenicity, while at the same time maintaining
the desirable level of food quality (Norton & Norton, 2010).
6.1. Example: egg white meringue
The previous discussion on foam structure (Section 3.1) illus-
trated the multitude of properties that must be considered when
evaluating protein functionality in foams. Discussion in Section 5
covered research related to the allergenic and bioactive properties
of proteins and peptides. These functional and biological consider-
ations will now be jointly considered using meringue as a case study.
A meringue is an egg white and sugar foam that is whipped to
various stages of rheological properties (soft peak or stiff peak) and
often baked to form the final food structure. This serves as a fairly
comprehensive model for food protein foam functionality evalua-
tion. Egg white consists of ovalbumin (54%), ovotransferrin
(12e13%), ovomucoid (11%) and a range of other proteins accounting
for the remaining 22e23% (Li-Chan & Nakai, 1989). Egg white
contains w10% w/w protein which puts ovalbumin at w1 mM.
A mixture of proteins, as is common in most food protein ingredients,
creates the chance for heterogeneity and multi-layers at the interface
(Le Floch-Fouéré et al., 2010) that will alter the overall foaming
properties (Glaser, Paulson, Speers, Yada, & Rousseau, 2007; Le Floch-
Fouéré et al., 2009). Sugars will increase the viscosity of the
continuous phase but are also know to alter denaturation tempera-
ture, protein aggregation and interfacial adsorption (McClements,
2002; Semenova, Antipova, & Belyakova, 2002). The transition
between soft and stiff peak is caused by increased whipping time and
most likely due to increased air phase volume but can also reflect
properties of the interfacial film, formation of a network in the
continuous phase, or some level of connection between the contin-
uous phase and interface (Foegeding et al., 2006; Pernell et al., 2002).
1861
Once the wet foam is formed, heat-induced changes in proteins will
determine if the foam structure remains or collapses during baking
(Fig. 2, Berry et al., 2009; Foegeding et al., 2006).
In targeting specific markets, it may be desirable to modify
current protein sources or utilize alternative protein sources for
improved allergenic profile or bioactive delivery; however, any
new or modified protein source would need to maintain satis-
factory food structure performance. As mentioned previously,
ovomucoid is considered the most problematic allergen in egg
white, and some groups are working toward generating ovomu-
coid depleted egg white fractions that retain similar foaming
properties to unmodified egg white (Tanabe et al., 2000). These
researchers exploited the solubility of ovomucoid in ethanol to
avoid extensive heating in preparing reduced ovomucoid egg
white ingredients, as excessive heat is generally detrimental to the
foaming functionality of egg white proteins (Tanabe et al., 2000).
Maillard modified protein sources could also be considered for
potential at reduced allergenicity (Taheri-Kafrani et al., 2009),
improved bioactive delivery (del Castillo et al., 2007) and
increased functionality (Oliver et al., 2006). Flavor and color would
be an obvious important consideration with any Maillard based
modifications. Heating of the meringue will clearly affect protein
structure and hence conformational epitopes. Sugar or sugar
substitutes used in the formulation can affect protein structure
during heating in a variety of ways with potential functional,
bioactive, and/or allergenic consequences. Heat-induced struc-
tural modifications are expected to be different for protein in the
continuous phase and that adsorbed at the interface (Mackie &
Macierzanka, 2010).
Taking the entire process into consideration, proteins function
in meringues at the following levels: a) interfacial film e formation,
structure and modification by other ingredients; b) continuous
phase e altering flow properties of a fluid phase and potentially
forming a network to create a solid phase; c) allow for changes in
interfacial film and continuous phase with heating that maintains
stability until the final structure is formed; and d) delivery of
bioactive properties and minimization or removal of allergenic
potential. As one can see, food proteins function in a multitude of
ways to create desirable and health food products.
Acknowledgments
“Paper No. FSR-10-36 of the Journal Series of the Department of
Food, Bioprocessing and Nutrition Science, North Carolina State
University, Raleigh, NC 27695-7624. Support from the North Caro-
lina Agricultural Research Service and Dairy Management Inc. as
administered by the Dairy Research Institute are gratefully
acknowledged. The authors would like to thank Ms. Paige Luck for
the technical assistance in preparing the manuscript. The use of
trade names in this publication does not imply endorsement by the
North Carolina Agricultural Research Service of the products named
nor criticism of similar ones not mentioned.
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