Current Opinion in Colloid and Interface Science 8 (2003) 365–370

Egg yolk protein gels and emulsions

V. Kiosseoglou*
Laboratory of Food Chemistry and Technology, School of Chemistry, Aristotle University of Thessaloniki, 54124 Thessaloniki, Greece

Abstract

Egg yolk remains a key ingredient of a number of food products. Yet, its main functional properties, e.g. emulsifying ability
and gel structure formation, upon heating, have not attracted the attention of too many researchers specializing in the area of food
colloids. It is not surprising then that there have been only very few major advances in the field over the period of the last few
years. These are discussed in the present review and include recent research findings on competitive adsorption between yolk
protein constituents at emulsion oil–water interfaces, and also on the relationship between yolk particle supermolecular structure
disorganization and the rheological properties of yolk-based emulsions and gel-network structures.
䊚 2003 Elsevier Ltd. All rights reserved.

Keywords: Yolk proteins; Adsorption; Gel formation; Rheological properties; Low density lipoproteins; Granules

1. Introduction subject are rare. Kiosseoglou w1x reviewed yolk chem-

Hen’s egg yolk can be found in a number of food
products such as mayonnaise and salad dressings, in
general, bakery products and cakes, custard, etc., being
an ingredient of high nutritional value with unique
sensory characteristics and excellent functionality. Thus,
the preparation and stability of yolk-based products
depend to a large extent on yolk constituent ability,
either to adsorb at oyw interfaces and form a strong and
cohesive film around oil droplets that stabilizes them
against coalescence, in the case of foods appearing in
the form of emulsions (e.g. mayonnaise), or to interact,
following heat treatment, and form network structures
exhibiting viscoelasticity in products such as creams and
omelet. During the preparation of certain products, e.g.
cakes, yolk constituents may have to function as emul-
sifiers and foaming agents as well as network structure
formers. Cake batter is a mixed colloidal system of an
emulsion, a foam and a suspension that, during baking,
is transformed into a solid foam, the cake, exhibiting
unique textural characteristics.
Although, however, yolk is a key ingredient of many
food systems, its functional properties have not received
the attention they deserve, possibly due to the material’s
complicated composition and structure. Reviews on the
*Tel.: q30-231-0-997834; fax: q30-231-0-997779.
E-mail address: kiosse@chem.auth.gr (V. Kiosseoglou).
istry and functionality, while structure network formation
by yolk, upon heating, was examined in a review by
Woodward w2x covering egg gelation. Both reviews
appeared some 10 or so years ago. Paraskevopoulou and
Kiosseoglou w3x very recently reviewed the functionality
of yolk protein concentrates prepared by extracting
cholesterol and other lipids. A recent review on egg
protein, both of albumen and yolk, was published by
Mine w4●x. The present work focuses on some aspects
of yolk functionality related to the role of isolated major
yolk fractions such as plasma (LDL and livetins) and
granules (HDL and phosvitin) in the stabilization of
oyw emulsions or in gel network formation. Emphasis
is placed on the functional behaviour of yolk proteins
since, as it appears from recent research findings, they
are the dominant yolk constituents in determining the
material’s functional properties. The majority of proteins
in yolk are organized into micellar and granular struc-
tures together with polar and non-polar lipid molecules.
Yolk functionality appears to depend on the type of
particle supermolecular structure (micellar or granular),
and also on the extent of structural disorganization
brought about by treatments such as pasteurization or
lipid extraction. One aspect of yolk functionality, there-
fore, that deserves attention is the effect of the degree
of supermolecular structure disorganization, and this
point will also be discussed in the review.

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366 V. Kiosseoglou / Current Opinion in Colloid and Interface Science 8 (2003) 365–370

2. Yolk protein gelation

Yolk coagulation or gelation, as a result of heating, is

an important functional property of the ingredient in the
preparation and texture modification of food products
such as sauces, creams, cakes, omelet, confectionery,
etc. Gel network structure formation by yolk is attributed
to its constituent protein denaturation, leading to molec-
ular interactions and the development of a hard and
rubbery structure w5x. Although the general theoretical
model, regarding gel network formation in the case of
heated protein solutions w6x, can be adopted to describe
the mechanism of yolk protein gelation, one should bear
in mind that yolk is not a pure protein solution, but
rather a dispersion of particles (LDL micelles and HDL
granules), where the neutral triglycerides are buried in
the particle interior, while the proteins dominate the
particle surface and in this way stabilize the system w3x.
The gelation of yolk, therefore, can be envisaged as a
process of particle destabilization brought about by
denaturation, upon heating, of particle-stabilizing yolk
protein molecules, leading to an interparticle network
formation. The system in this respect resembles that of
a protein-stabilized concentrated emulsion that gels fol-
lowing heat treatment.
Apolipoproteins of LDL micelles appear to dominate
the process of yolk gelation. As reported by Anton et
al. w7●●x similar gelation patterns were followed by a
yolk plasma solution and liquid yolk, while the granules
exhibited a completely different behaviour and were less
effective as gel network formation agents. This differ-
ence in behaviour, according to the authors, should be
the result of the more labile nature of LDL micelles and
of the ease with which micellar apolipoprotein and
livetin molecules denature at relatively low temperatures.
Granular proteins, on the other hand, are less sensitive
to heat, a behaviour attributed to their more globular
structure and to complexes between high density apoli-
poprotein molecules and phosvitin in the granular struc-
ture w8x.
Heat treatments similar to those applied during spray-
drying may also destabilize particle supermolecular
structure leading yolk dispersions in water to exhibit
‘weak’ gel properties. A similar behaviour was observed
for yolk protein concentrates obtained by lipid extraction
of yolk w9x. The ‘weak’ gel network at room tempera-
tures, where physical forces dominate protein interac-
tions, turns into a real gel, probably due to protein
denaturation and the development of covalent disulfide
forces between interacting molecules w10x.
Another aspect of yolk protein gelation behaviour that
deserves attention is the way it is modulated by the
presence of low-molecular weight compounds, particu-
larly emulsifiers. Yolk protein gelation is influenced by
hydrophilic surfactants such as Tween and gels produced
upon heating of spray-dried yolk, in presence of Tween
Fig. 1. Development of G9, following heating to 75 8C and cooling to
5 8C, as a function of protein concentration for spray dried yolk (h)
and for yolk protein concentrates prepared by extraction with etha-
nolywater (d) or petroleum etheryethanol (m). Sample lipid content:
spray dried yolk: 60%, extracted with ethanolywater: 32.2%, extracted
with petroleum etheryethanol: 6.5% (wyw). Frequency: 1.5 Hz; strain:
0.2 (from Ref. w9x).
20, exhibit higher fracture stress values w11x probably
as a result of excluded volume effects andyor surfac-
tant–apolipoprotein interactions. A similar behaviour
was also observed for pure proteins such as b-lactoglob-
ulin by Dickinson and Hang following addition of Tween
w12x.
The presence of native yolk lipids or fat incorporated
in the form of emulsified oil droplets appears to influ-
ence the yolk gel rheological properties but in a different
way. Yolk protein concentrates having a relatively high
lipid content produce gel networks at low protein con-
centrations and full-fat spray-dried yolk forms weak gels
even at very low protein levels (1.9% wyv) suggesting
that the yolk lipid molecules are somehow involved in
gel structure formation w9x (Fig. 1). Emulsified oil
droplets of an average size of 1 mm, on the other hand,
act as inactive fillers of egg yolk gels. A plausible
explanation of this effect is that the LDL micelles of
plasma that dominate the gelation process of yolk and
their apolipoproteins, which are over-represented at the
oil–water interface, as a result of their flexibility, cannot
be involved in cross-links to enhance protein–oil droplet
interactions due to orientation of their hydrophobic
groups towards the oil phase w7●●x.
3. Yolk proteins at oyw interfaces
The preparation and long-term stability of food emul-
sions such as mayonnaise, salad creams and egg-based
 V. Kiosseoglou / Current Opinion in Colloid and Interface Science 8 (2003) 365–370
sauces and creams depend to a significant extent on egg
yolk constituent ability to aid in the reduction of
interfacial tension between the two phases, resulting in
a fine dispersion and form an adsorbed film around the
oil droplets that offers protection against coalescence
and ultimate phase separation during prolonged storage.
The composition and fine structure of adsorbed pure
protein films, the interfacial rheological properties and
their influence on colloidal stability have been the
subject of considerable debate over the last two decades,
and although some progress has been achieved in this
area there are still many points that require clarification,
one of them being the connection between the adsorbed
film properties with the stability of the bulk systems
w13x. This situation becomes even more complicated in
the case of egg yolk proteins, which constitute a very
diverse mixture of molecules differing both in structure
and flexibility. Furthermore, approximately 90% of these
proteins are organized into supermolecular structures
exhibiting marked differences in size, structure stability
and composition.
Melnikov w14●●x applied dynamic drop tensiometry to
determine the kinetics of yolk adsorption at the oyw
interface and the viscoelastic modulus as they are
influenced by the solution pH. His observation shows
that interfacial tension reaches a minimum at pH values
close to the isoelectric region of yolk proteins, which
was also reported in a previous study by Anton and
Gandemer w15x, a fact that points to the role of protein
charges in determining yolk protein adsorption. Accord-
ing to Melnikov, however, the pH does not appear to
influence the viscoelasticity of egg yolk interfacial films.
Egg yolk constituent adsorption at the oyw interface
occurs in a step-wise manner indicating that substantial
molecular interactions, rearrangements and partial
replacement of various protein fractions may take place
leading to modification of film structure and viscoelas-
ticity. This was expected since, when the components
of a diverse mixture of proteins, differing in molecular
structure and flexibility, compete for space at oyw
interface with low-molecular weight surface-active mol-
ecules such as phospholipids and cholesterol, competi-
tive adsorption will take place, that requires time for
equilibrium to be reached.
Yolk LDL micelles, due to their rather unstable nature,
are easily disorganized when they come into contact
with oil droplet surfaces, and their apolipoprotein con-
stituents adsorb and spread readily at the interface aided
in this by their high structure flexibility w16,17●,18–20x.
According to Mine w17●x, preferential adsorption occurs
between the micellar protein constituents, and as a result
of this three LDL-polypeptides (64, 43 and 19 kDa) do
not adsorb at all at the interface. Additionally, phospho-
lipid and cholesterol adsorption depends on LDL con-
centration with the ratio of phosphatidylcholine over
phosphatidyl-ethanolamine increasing with increasing
367
LDL concentration, a result that emphasizes the role of
protein–lipid interactions in the development of
adsorbed yolk lipoprotein films around the oil droplets.
Most of the research papers published in the last 1–
5 years stressed the importance of micellar apolipopro-
teins in the development of adsorbed films around the
oil droplets of yolk-based emulsions, along with other
yolk proteins (livetins, granular apolipoproteins and
phosvitin) w21,22x although there is one paper w23x
reporting that granular lipovitellines are the main com-
ponents found at the interface in spite of the granule
low solubility, under low ionic strength conditions.
Since, however, yolk protein adsorption at oyw inter-
faces depends on parameters such as pH and NaCl
concentration, homogenization conditions, etc., it is not
surprising that the relative contribution of yolk protein
constituents to the formation of adsorbed films may
differ as stressed by LeDenmat et al. in a recent paper
w24●●x. Granular protein adsorption in oyw emulsions
depends heavily on pH, and emulsions of pH 4 exhibit
a higher protein surface load than that of pH 7 or 9.
This was attributed to lipoprotein dimer formation at the
acidic pH w25x. Compared with phosvitin, granule lipo-
proteins are more surface active and displace the former
more effectively at neutral pH than at pH 4.0, a fact
that emphasizes the importance of phosvitin negative
charge in determining its affinity to the oyw interface
w26x. According to Anton et al. w27x, granules may
adsorb either in their native form or after disruption,
following NaCl addition. Disrupted granules are more
effective in producing finer and more homogeneous
emulsions.
One interesting aspect of yolk protein adsorption is
their tendency to displace other proteins of a more
globular nature from the interface. Thus, yolk proteins
being highly surface active can very effectively displace
milk proteins from emulsion interfaces. Both whey
proteins w28●x and caseinate w29x may be displaced by
LDL or granule lipoproteins in emulsions, depending on
the nature of oil phase. This is attributed to the high
penetrating ability of yolk lipoprotein molecules.
Finally, cholesterol removal from yolk may influence
the lipoprotein adsorption behaviour. Thus, cholesterol
extraction from LDL results in thicker adsorption films
around the oil droplets of emulsions, due to apoprotein
aggregation w30x. The adsorption behaviour of low-in-
cholesterol yolk depends on the method of lipid extrac-
tion and was attributed to structural changes of yolk
proteins brought about by the extraction process w31x.
4. Stability and rheology of egg yolk emulsions
Properties of protein-based emulsions such as long-
term stability and rheological behaviour and texture are
intimately related to interactions taking place among
adsorbed protein molecules either within the interfacial
368 V. Kiosseoglou / Current Opinion in Colloid and Interface Science 8 (2003) 365–370
Fig. 2. Influence of pH andyor NaCl addition on average droplet size
and creaming ‘delay period’ of yolk emulsions (10% corn oil, 1%
yolk). Numbers in parenthesis are ‘delay periods’ expressed in min
(from Ref. w10x).
film or between neighbouring oil droplets w32x. Concen-
trated yolk emulsions, such as full-fat mayonnaise, are
practically stable against creaming over storage periods
of years, due to close oil droplet packing and deforma-
tion that prevent droplet movement and serum separa-
tion. The rheological properties of this system depend
heavily on the size of the oil droplets as well as on oil
volume fraction w33x, although other parameters, such
as the concentration and structure of yolk proteins,
should also have a significant effect on mayonnaise
rheology w34x. Less concentrated yolk emulsions, such
as salad creams and sauces, tend to cream on storage
and have to be stabilized with the aid of polysaccharides
such as xanthan gum. These systems, in contrast to
biopolymer gels, exhibit phase angle, d, values between
98 and 128 indicating a structure heavily dependent on
yolk protein content and structure as well as on oil
droplet size w35x.
Stability against creaming of yolk-based emulsions
with a low oil fraction, in the absence of polysacchar-
ides, appears to be largely determined by steric interac-
tions due to adsorbed LDL apolipoproteins w24●●x.
Granular proteins may also adsorb at the oyw interface
of yolk emulsions, along with LDL and enhance the
stability of the system, provided the granular structure
is disorganized by the addition of 0.6 M NaCl and
bridging flocculation, due to intact adsorbed granules is
prevented w10x (Fig. 2).
As was pointed out above, the structure of yolk
particles influences the rheology of yolk-stabilized emul-
sions. Yolk structure alterations may take place as a
result of processes such as spray-drying or lipid extrac-
tion. Spray-dried yolk produces emulsions exhibiting
higher viscoelasticity compared to those of native yolk
w36x. According to Moros et al. w37x, the spray-drying
process of a low-in-cholesterol yolk confers a marked
gel-like behaviour to the product, which in turn influ-
ences the viscoelasticity of 70% oyw emulsions. Fur-
thermore, thermal treatment of highly flocculated yolk
emulsions results in an enhancement of viscoelastic
parameter values, provided that emulsion breakdown is
avoided. Egg yolk stabilized emulsions are, however,
less susceptible to emulsion gel enhancement compared
with milk protein systems w38x. This difference in
behaviour was attributed to the fact that at 67 8C, which
was the maximum temperature reached, yolk proteins
were not expected to become further denatured since
most of them require higher temperatures to exhibit
structure alterations.
5. Conclusions
Adsorption at oil–water interfaces of emulsion oil
droplets or molecular denaturation, upon heating, leading
to gel network structure formation, are the key functional
properties of yolk proteins depending, among other
factors, on yolk particle (LDL micelle and granule)
supermolecular structure disorganization brought about
by surface forces, salt addition or processes such as
homogenization, spray-drying, pasteurization or lipid
extraction. LDL micelles and granules, due to their
differences in composition and structure, exhibit a totally
different behaviour upon adsorption, or heating and
gelation, leading to the appearance of phenomena such
as competitive adsorption between their constituent pro-
teins in emulsions and mixed gel structure formation,
respectively. Recent research findings emphasize the
dominant role of LDL micellar proteins either in emul-
sion formation and stabilization or in gel network
structure development. Granular proteins, on the other
hand, appear to play a secondary role in these systems
although one should keep in mind that their behaviour
is modulated by the state of the granular structure. Once
granules are disorganized, their constituent proteins are
liberated and take part in interfacial film formation and
emulsion stabilization as well as in gel structure devel-
opment, in a more efficient way. Further research is
needed, however, to clarify their role both in emulsions
and in gels. Yolk is one of a number of ingredients
found in food products. Due to interactions with other
food biopolymers such as proteins of animal or plant
origin, its functional performance could be modulated.
In creams where yolk may be used along with milk,
yolk proteins appear to displace whey proteins and
casein from oil surfaces due to their more flexible
structure. In products such as cakes and confectionery,
interactions of yolk proteins with other biopolymers
such as egg white proteins, gluten or added surfactants
 V. Kiosseoglou / Current Opinion in Colloid and Interface Science 8 (2003) 365–370
are bound to determine the product structure and textural
properties. Research in this area is very difficult to
conduct as a result of the complexity of the systems
under study. The task becomes even more formidable in
view of the complexity of the composition and the
structure of the yolk itself. A very recent attempt to
isolate and evaluate the functionality of major yolk
apolipoproteins could be the first step in the better
understanding of yolk functionality both in emulsions
and in gels.
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