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Protein-stabilized emulsions
David Julian McClements*
Biopolymers and Colloids Laboratory, Department of Food Science, University of Massachusetts, Amherst, MA 01003, USA
Available online 19 October 2004
Abstract
Proteins are widely used as emulsifiers to facilitate the formation, improve the stability and provide specific physicochemical properties to
oil-in-water emulsions. There have been a number of recent advances in the understanding of the ability of various types of proteins to provide
these functional properties. This article focuses on the influence of solution composition (pH, ionic strength, sugars, polyols, surfactants,
biopolymers) and environmental stresses (heating, chilling, freezing, drying) on the stability of globular protein stabilized emulsions.
D 2004 Elsevier Ltd. All rights reserved.
Keywords: Emulsions; Proteins; Surface denaturation; Thermal denaturation
1. Introduction
Many proteins are surface-active molecules that can be
used as emulsifiers because of their ability to facilitate the
formation, improve the stability and produce desirable
physicochemical properties in oil-in-water emulsions [1 ].
Proteins adsorb to the surfaces of freshly formed oil
droplets created by homogenization of oilwaterprotein
mixtures, where they facilitate further droplet disruption by
lowering the interfacial tension and retard droplet coalescence by forming protective membranes around the
droplets [2]. The ability of proteins to generate repulsive
interactions (e.g., steric and electrostatic) between oil
droplets and to form an interfacial membrane that is
resistant to rupture also plays an important role in
stabilizing the droplets against flocculation and coalescence during long-term storage [3,4 ,5 ].
The development of protein-stabilized emulsions with
improved or novel physicochemical properties relies on
understanding the interfacial behavior of adsorbed proteins, and on elucidating the relationship between
interfacial characteristics and bulk physicochemical properties of emulsions. A great deal of research has been
carried out to develop a better fundamental understanding
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2.4. Homogenization
One of the most important roles of emulsifiers is to
facilitate the formation of small emulsion droplets during
homogenization of the oil and aqueous phases. An effective
emulsifier should rapidly adsorb to the freshly formed
droplet surfaces, reduce the interfacial tension by an
appreciable amount to facilitate droplet disruption and
provide a protective coating that prevents the droplets from
aggregating with their neighbors [2]. Protein emulsifiers
differ in the rate at which they adsorb to droplet surfaces
during homogenization, in the minimum amount that is
required to saturate the droplet surfaces, and in their ability to
protect droplets against coalescence under different environmental conditions [19]. For example, casein micelles adsorb
more rapidly to droplet surfaces than individual casein
molecules during high pressure valve homogenization, but
more protein is required to saturate the droplet surfaces for
casein micelles than individual casein molecules. The
amount of total protein present also plays a major role in
determining the stability of the droplets to aggregation
during homogenization. It is convenient to divide the
influence of emulsifier concentration on droplet size into
two regions [18 ]:
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Fig. 2. Effect of (a) potassium chloride and (b) calcium chloride on mean
particle diameter of diluted 7 wt.% soybean oil-in-water emulsions
stabilized by WPI. The multivalent counter-ion is more effective at
destabilizing the emulsions due to ion-binding and screening effects.
a protein-stabilized emulsion to change the pH dependence of the f-potential of the droplets, thereby
changing the range of pH values that the emulsion is
stable to flocculation [38 ,39].
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3.4. Biopolymers
Protein-stabilized oil-in-water emulsions may contain
one or more types of biopolymer in the continuous phase.
These biopolymers could be a fraction of the protein used as
an emulsifier that did not adsorb to the droplet surfaces
because they were already saturated with protein, or they
could be other functional ingredients, such as thickening
agents or gelling agents. These biopolymers may interact
with the adsorbed proteins, either directly or indirectly, and
influence the stability of the emulsion through a variety of
mechanisms [38 ].
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4. Conclusions
There have been significant advances in our understanding of the factors that influence the functionality of
proteins in oil-in-water emulsions. This article has mainly
focused on advances in the understanding of the influence of
solution composition and environmental stresses on protein
functionality. Improved knowledge of these effects should
facilitate the rational and systematic design and production
of emulsion-based products.
References and recommended reading
[1] W. Norde. Colloids and Interfaces in Life Sciences, Marcel Dekker,
New York, NY, 2003.
An excellent up-to-date introduction and overview of the molecular and
physicochemical basis of protein functionality in biological systems.
! of special interest
!! of outstanding interest
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D.J. McClements / Current Opinion in Colloid & Interface Science 9 (2004) 305313
Excellent overview of some important factors that determine droplet
coalescence in protein stabilized emulsions, such as mechanical forces,
surfaces and air bubbles.
[18] S. Tcholakova, N.D. Denkov, I.B. Ivanov, B. Campbell. Interrelation
between drop size and protein adsorption at various emulsification
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Shows that droplet surfaces that are not completely saturated by protein are
more unstable to droplet coalescence.
[19] D.J. McClements. Food Emulsions: Principles, Practice and Techniques, CRC Press, Boca Raton, Florida, 1999.
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Evidence that homogenization of BSA-stabilized hexadecane-in-water
emulsions induces structure modification of the nonadsorbed protein,
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physicochemical properties of model nutritional beverages based on
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citrate on physicochemical properties of whey protein-stabilized oilin-water emulsions containing CaCl2, J. Agric. Food Chem. 50
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