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Utilization of Natural
Emulsifiers to Form and
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Stabilize Emulsions
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205
FO08CH11-McClements ARI 31 January 2017 9:55
INTRODUCTION
Many consumer products are structured using oil-in-water emulsions, either during their pro-
duction or in the final product form, e.g., food, nutritional supplements, and pharmaceutical,
personal care, and cosmetic products (Gutierrez et al. 2008; McClements 2010, 2012; Sagalowicz
& Leser 2010). In food products, the fat droplets provide desirable physicochemical and sensory
attributes such as appearance, texture, mouthfeel, and flavor (McClements 2015a). In addition,
they may also be used to encapsulate, protect, and deliver lipophilic bioactive compounds, such
as flavors, colors, vitamins, nutrients, nutraceuticals, antimicrobials, and antioxidants (Fathi et al.
2012, McClements 2010, Sagalowicz & Leser 2010, Velikov & Pelan 2008).
Oil-in-water emulsions are thermodynamically unstable systems that have a tendency to sep-
arate back into their component oil and water phases over time. To manufacture commercial
products with long shelf lives and resistances to environmental stresses, stabilizers are therefore
Annu. Rev. Food Sci. Technol. 2017.8:205-236. Downloaded from www.annualreviews.org
required (McClements 2015a). Numerous types of stabilizers are available to improve emulsion
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stability, including emulsifiers, thickeners, weighting agents, and ripening inhibitors. In this arti-
cle, we primarily focus on emulsifiers because these ingredients are critical to the proper perfor-
mance of any emulsion-based product. Many of the most effective emulsifiers currently used in
food products are synthetic, such as sorbitan esters, fatty alcohol ethoxylates, and sucrose esters
(Hasenhuettl 2008, Kralova & Sjoblom 2009, Stauffer 1999). However, the demand for the use
of natural and sustainable ingredients in food products is growing because of increasing aware-
ness of the importance of healthy eating and environmental sustainability (Karaca et al. 2015,
Lam & Nickerson 2013). For this reason, many food manufacturers are trying to replace syn-
thetic emulsifiers with natural alternatives, as well as trying to replace animal-based ingredients
with plant-based ingredients (Baines & Seal 2012). This article briefly discusses the physicochem-
ical basis of emulsifiers’ ability to form and stabilize oil-in-water emulsions, and then provides an
overview of different types of natural emulsifiers that can be used in foods, such as phospholipids,
biosurfactants, proteins, and polysaccharides.
EMULSIFIER CHARACTERISTICS
An emulsifier should have a number of desirable characteristics if it is going to be utilized within
the food industry as well as in other industries. Some of these characteristics are related to the
physicochemical properties of the emulsifier, whereas others are related to more practical and eco-
nomic factors. In general, an emulsifier plays two major roles in the creation of emulsion-based
products: emulsion formation and emulsion stability (Figure 1). The most important character-
istics of any emulsifier are (a) the ability to rapidly adsorb to the surfaces of the droplets created
during homogenization; (b) the ability to reduce the interfacial tension by an appreciable amount
so as to facilitate further droplet disruption; and (c) the ability to form a protective coating around
the droplets that prevents their aggregation by generating strong repulsive forces, such as steric
or electrostatic repulsion (McClements 2015a). The major factors affecting the formation and
stability of emulsions have been reviewed in detail elsewhere (McClements & Gumus 2016) and
thus are not considered further here. However, some of the key parameters that can be used to
compare the effectiveness of different natural emulsifiers are summarized.
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Requirements: Requirements:
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value (SAT ) as the surfactant concentration increases from zero to a value above that, causing
saturation. The ability of oil droplets to be disrupted during homogenization depends on the
interfacial tension, and thus those natural emulsifiers that are more effective at reducing the
interfacial tension (higher SAT ) should lead to smaller droplets.
Surface Activity
The surface activity of an emulsifier is an indication of its affinity for an oil-water interface:
the higher the surface activity, the stronger the affinity. The surface activity is taken to be the
reciprocal of the emulsifier concentration required to reach SAT /2: SA = 1/c1/2 (McClements
2015a). Emulsifiers with a high surface activity tend to adsorb to oil droplet surfaces at lower
concentrations than those with low surface activity and tend to stick more strongly. Consequently,
in a system containing a mixture of emulsifiers, the ones with the highest surface activities tend to
adsorb to the interfaces preferentially.
Surface Load
The surface load () of an emulsifier is the mass adsorbed per unit surface area and is related to
emulsion properties by the expression
6 · sat · ϕ
cS = . 1.
d 32
Here, cS is the emulsifier concentration (in kg/m3 ), sat is the surface load (in kg/m2 ), ϕ is the
disperse phase volume fraction (dimensionless), and d32 is the surface-weighted mean droplet
diameter (in m). This expression assumes the droplet surfaces are saturated with emulsifier, and
the disruptive forces generated by the homogenizer do not limit the size of the droplets formed.
Thus, more emulsifier is required to produce emulsions with smaller droplet sizes, higher droplet
concentrations, or higher surface loads. For natural emulsifiers, the surface load typically follows
Lecithin
Saponins
4 Gum arabic
2
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1
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0
0 1 2 3 4 5
Emulsifier concentration (%)
Figure 2
The effectiveness of different emulsifiers can be compared by plotting mean particle diameter (d32 ) versus
emulsifier concentration. Data from Ozturk et al. (2015a).
the general trend of polysaccharides > flexible proteins > globular proteins > biosurfactants. Thus,
a greater amount of a polysaccharide is typically required to form an emulsion than a protein or
a biosurfactant. This conclusion is supported by experimental measurements of the droplet size
versus emulsifier level (Figure 2).
Adsorption Kinetics
The rate at which the droplet surfaces are covered by emulsifier molecules during homogenization
is important because it influences the efficiency of droplet disruption (by decreasing the interfacial
tension) and the kinetics of droplet coalescence (by increasing repulsive interactions). Ideally, the
emulsifier molecules should rapidly move to the droplet surfaces and become strongly attached.
Natural emulsifiers vary considerably in their adsorption kinetics depending on their molecular
dimensions and surface chemistries. Typically, large emulsifiers (such as polysaccharides) adsorb
more slowly than small ones (such as biosurfactants). In general, the saturation surface pressure,
surface activity, surface load, and adsorption kinetics of natural emulsifiers vary considerably,
which leads to differences in their ability to form and stabilize emulsions.
NATURAL EMULSIFIERS
The major types of natural emulsifier currently used in the food industry, or that have potential
for application in foods, are reviewed in this section.
Phospholipids
Phospholipids are amphiphilic molecules naturally found in the cell membranes of animals, plants,
and microorganisms, which are widely used as emulsifiers in foods (Erickson 2008).
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Molecular and physicochemical characteristics. Phospholipids consist of two fatty acids (the
nonpolar tail) and a phosphoric acid moiety attached to a glycerol backbone (the polar head).
The fact that phospholipids have polar and nonpolar parts on the same molecule means they can
adsorb to oil-water interfaces and act as emulsifiers (Pichot et al. 2013). Phospholipids may form
a single layer around oil droplets, where the fatty acid tails protrude into the oil droplets and
the hydrophilic head points toward the water, or they may form multiple layers with each layer
consisting of two phospholipids lined up head-to-head and tail-to-tail (Liu et al. 2015, Pichot
et al. 2013). The type of structure formed depends on phospholipid type and concentration, and
impacts emulsion formation and stability.
Phospholipid-based emulsifiers used in the food industry are usually referred to as lecithins
(Klang & Valenta 2011, Kralova & Sjoblom 2009) and may be extracted from numerous sources,
including soybeans, eggs, milk, rapeseed, canola seed, cottonseed, and sunflower (Bueschelberger
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2004). Food lecithins typically consist of mixtures of phospholipids with different head and tail
groups, as well as other types of lipids, such as triglycerides, glycolipids, and sterols (Guiotto et al.
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2013). Nevertheless, they can be fractionated to form ingredients with different compositions,
purities, and functionalities. The most common phospholipids in food-grade lecithins are phos-
phatidylcholine (PC), phosphotidyletanolamine (PE), phosphatidylinositol (PI), and phosphatidic
acid (PA) (Erickson 2008). In nature, the nonpolar tails typically consist of two fatty acids that
may have different numbers of carbon atoms and double bonds. Nevertheless, one of the fatty
acids may be chemically or enzymatically removed to form lysolecithins with different functional
properties than conventional lecithins (Table 1) (Casado et al. 2012).
Table 1 Comparison of properties of natural emulsifiers isolated from various sources that may be utilized within the
food industry
Emulsifier Sources Molecular properties Emulsion properties References
Phospholipids
Lecithin Soybeans, milk, eggs, Consisting of polar Form small droplets at low (Klang & Valenta
sunflower, cottonseed, (phosphoric acid moiety levels via high-energy 2011, Ozturk
canola seed head group) and nonpolar emulsification methods. et al. 2014)
(two fatty acids tail group) Unstable under acidic
on the same molecule conditions (pH < 3) and high
ionic strength (>100-mM
NaCl). Less sensitive to high
temperatures
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Lyso-lecithin Enzymatical and/or Consisting of polar Forms small droplets at low (Cabezas et al.
chemical modification of (phosphoric acid moiety levels via high-energy 2015, Casado
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raw lecithin head group) and nonpolar emulsification methods. et al. 2012)
(one fatty acid tail group) on Unstable under acidic
the same molecule conditions (pH < 3) and high
ionic strength (>100-mM
NaCl). Less sensitive to high
temperatures
Biosurfactants and bioemulsifiers
Saponins Extracts isolated from the Consisting of hydrophilic Form fairly small droplets at (Mitra & Dungan
bark of the Quillaja (e.g., sugar groups) parts and low levels via high-energy 1997, Ozturk
saponaria tree hydrophobic (e.g., emulsification methods. et al. 2014)
triterpenoid rings) parts on Unstable under acidic
the same molecule conditions (pH < 3) and high
ionic strength (>300-mM
NaCl). Stable to high
temperature (up to 90◦ C)
Sophorolipids Produced by microbial Consisting of the hydrophilic Form fine droplets at various (de Oliveira et al.
fermentation processes sophorose group concentrations via 2015, Elshafie
utilizing suitable yeast (disaccharide structures) and emulsification methods. et al. 2015, Xue
strains (e.g., Candida hydrophobic hydrocarbon Stable over a wide range of et al. 2013)
batistae) and substrates tail (a fatty acid chain) on the pH values (2–12), at high
(e.g., carbon and same molecules. More temperatures (40–100◦ C),
nitrogen sources) hydrophobic than other and at high ionic strengths
biosurfactants (13–15% salinity)
Rhamnolipids Produced by microbial Consisting of one or two Form small droplets at various (Deepika et al.
fermentation processes polar rhamnose units concentrations via 2016, Henkel
utilizing optimized (containing carboxylic acid emulsification methods. et al. 2012,
microbial strains, group) and one nonpolar Unstable under alkalic Nitschke et al.
fermentation conditions, fatty acid chain (composed conditions (pH > 8) and at 2010)
and substrates of β-hydroxylalkanote) high temperatures (>80◦ C).
Stable to high ionic strengths
(up to 800-mM NaCl)
(Continued )
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Table 1 (Continued )
Emulsifier Sources Molecular properties Emulsion properties References
Mannoproteins Cell wall of Saccharomyces Consisting of a protein Form stable emulsions at (Alcantara et al.
cerevisiae and backbone attached with two relatively high concentration 2013, Araujo
Saccharomyces uvarum types of mannan chains: >2%. Emulsions stable et al. 2014,
from baker or spent beer (a) long branched bulky across a broad range of pH (3 Barriga et al.
or wine (brewer’s) yeasts chains (40 to 100 mannose to 11) in some studies but 1999, Cameron
units) that may be was found to be pH sensitive et al. 1988, Dikit
phosphorylated; (b) shorter in another study. Emulsions et al. 2010,
chains (1 to 5 mannose units) stable under different salt Torabizadeh
that are not phosphorylated conditions (up to 5% sodium et al. 1996)
chloride and 0.1% calcium
chloride and magnesium
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chloride)
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Proteins
Whey protein Whey, milk Mixture of globular proteins Form fairly small droplets at (McClements
MW ≈ 18 kDa; pI ≈ 5; Tm ≈ low concentrations. Unstable 2004, Ozturk
80◦ C at pH near pI (around pH 5), et al. 2015a)
at high ionic strengths, and
at high temperatures (>Tm )
β- Major whey protein of Globular protein Form fairly small droplets at (Ali et al. 2016)
Lactoglobulin cow and sheep’s milk MW ≈ 18.4 kDa; pI ≈ 5.4; low concentrations. Unstable
Tm ≈ 83◦ C at pH near pI, at high ionic
strengths, and at high
temperatures (>Tm )
α- Isolated from whey Globular protein Form fairly small droplets at (Lam &
Lactalbumin protein MW ≈ 14.2 kDa; pI ≈ 4.4; low concentrations. Unstable Nickerson 2015)
Tm ≈ 83◦ C at pH near pI, at high ionic
strengths, and at high
temperatures (>Tm )
Bovine serum Isolated from whey Globular protein Unstable at pH near pI, at (Park et al. 2015)
albumin protein of cow’s milk MW ≈ 66.3 kDa; pI ≈ 5.1; high ionic strengths, and at
Tm ≈ 75◦ C high temperatures (>Tm )
Lactoferrin Isolated from whey Globular glycoprotein Form fairly small droplets at (Teo et al. 2016)
protein MW ≈ 80 kDa; pI ≈ 8; Tm ≈ low concentrations. Unstable
60 and 85◦ C at pH near pI, at high ionic
strengths, and at high
temperatures (>Tm )
Caseinates Milk Mixtures of flexible proteins Form small droplets at low (Medina-Torres
MW ≈ 24 kDa; pI ≈ 5 concentrations. Unstable at et al. 2009)
pH near pI and at high ionic
strengths. Stable to high
temperatures
αs -Casein Milk Flexible protein Unstable at pH near pI and at (Kaminogawa
MW ≈ 23.6 kDa; pI ≈ 5.1 high ionic strengths. Stable et al. 1987)
to high temperatures
(Continued )
Table 1 (Continued )
Emulsifier Sources Molecular properties Emulsion properties References
β-Casein Milk Flexible protein with higher Unstable at pH near pI and at (Dickinson et al.
adsorption rate to oil-water high ionic strengths. Stable 1988)
interface. to high temperatures
MW ≈ 24.0 kDa; pI ≈ 5.5
Egg protein Egg or yolk Mixture of globular proteins Can form fine droplets at (Chang et al.
various concentrations. 2016)
Unstable at pH near pI, at
high ionic strengths
(>100-mM NaCl), and at
high temperatures (>90◦ C)
Ovalbumin Main protein in egg white, Globular protein Unstable at pH near pI, at (Niu et al. 2016)
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Table 1 (Continued )
Emulsifier Sources Molecular properties Emulsion properties References
Beet pectin Isolated from the Consisting of branched Form micron or submicron (Funami et al.
extraction of sugar anionic hydrophilic droplets at high 2011, Leroux
polysaccharide and surfactant-to-oil ratio via et al. 2003)
hydrophobic ferulic acid high-energy emulsifier
groups methods. Stable over a wide
range of environmental
stresses (pH, ionic strength,
and temperature)
Citrus pectin Mainly extracted from Consisting of branched Form micron or submicron (Leroux et al.
citrus fruits anionic hydrophilic droplets at high 2003)
polysaccharide and surfactant-to-oil ratio via
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Emulsion stability. Phospholipid-coated lipid droplets are mainly stabilized against aggregation
by electrostatic repulsion arising from their electrical charge (Ozturk et al. 2014, Washington
et al. 1989). Different phospholipids have different electrical characteristics depending on the na-
ture of their head groups (Washington 1996). For example, PI and PA are anionic, whereas PC
and PE are zwitterionic, with the overall charge depending on solution pH relative to the pKa
values of the ionizable groups. Consequently, the electrical charge on oil droplet surfaces can be
tailored using different types and ratios of phospholipids (Washington et al. 1989). Under basic
and neutral pH conditions, lecithin-coated droplets typically have a relatively high negative charge
(Figure 3a), which helps to prevent droplet aggregation by generating a strong electrostatic repul-
sion. However, when the pH is reduced the droplet charge becomes progressively less negative,
then passes through zero, and then becomes slightly positive (Ozturk et al. 2014, Washington
1996). As a result, lecithin-coated oil droplets tend to be prone to aggregation under highly acidic
conditions (Figure 3b). For example, lecithin-coated oil droplets were shown to be stable to ag-
gregation from pH 8 to pH 3, where they had a high charge, but were unstable at pH 2, where
they had a low charge (Ozturk et al. 2014).
The fact that lecithin-coated droplets are primarily stabilized by electrostatic repulsion means
that they are highly susceptible to salt addition (Komaiko et al. 2016, Washington 1996). At neutral
pH, where the droplets have a high negative charge, rapid aggregation occurs when a sufficiently
high level of monovalent (Na+ ) or divalent (Ca2+ ) ions is added to the system due to electrostatic
screening and/or bridging effects (Komaiko et al. 2016, Ozturk et al. 2014, Washington 1996).
Typically, much lower levels of multivalent counter-ions (approximately 3-mM Ca2+ ) are required
to promote aggregation than monovalent counter-ions (approximately 100-mM Na+ ) because
the former are more effective at increasing the ionic strength and binding to oppositely charged
droplets. Interestingly, the addition of high levels of multivalent cations to emulsions containing
lecithin-coated droplets may actually cause the charge to change from negative to positive, which
can cause the emulsions to become more stable to aggregation (Washington 1996). At neutral pH
in the absence of salt, lecithin-coated oil droplets are relatively stable to thermal processing (30
to 90◦ C, 30 min) because of the strong electrostatic repulsion between them (Ozturk et al. 2014).
a 50 b
Lecithin 103 Lecithin
102
ζ-potential (mV)
10
–10
101
–30
100
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–50
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–70 10–1
2 3 4 5 6 7 8 2 3 4 5 6 7 8
pH pH
Figure 3
Change in (a) droplet charge (ζ-potential) and (b) mean particle diameter with pH for different kinds of natural emulsifiers:
phospholipids (lecithin), quillaja saponins (Q-Naturale
R
), gum arabic, and whey protein isolate.
The stability of lecithin-coated oil droplets depends on phospholipid type, e.g., the ratio of PC
to PE (Guiotto et al. 2013, Komaiko et al. 2016). Phospholipids with high PC levels were reported
to produce smaller oil droplets (Cabezas et al. 2012, Komaiko et al. 2016). Some phospholipids may
also retard the oxidation of emulsified lipids, which was attributed to their free radical scavenging
capacity (Choe et al. 2014, Pan et al. 2013).
Many lecithins are not good emulsifiers when used alone because they are too lipophilic, i.e.,
they have relatively low or intermediate HLB numbers. However, their performance as emulsifiers
can be improved by mixing them with other natural emulsifiers, e.g., caseins (Garcia-Moreno et al.
2014, Xue & Zhong 2014), whey proteins (Frede et al. 2014), and monoacylglycerols (Zou & Akoh
2013). Their performance can also be improved by mixing them with cosolvents, such as ethanol
(Wiacek & Adryanczyk 2015). The performance of lecithins can also be improved by removing
one of the fatty acid tails to create lysolecithins (Casado et al. 2012, Choi et al. 2011). The stability
of lecithin-coated oil droplets can also be increased by using electrostatic deposition to coat them
with oppositely charged polyelectrolytes (Ogawa et al. 2003a,b, 2004).
Applications. Ultrafine lecithin-coated oil droplets have been used to improve the bioavailability
of conjugated linoleic acids (Heo et al. 2016) and to encapsulate and deliver oil-soluble vitamins
(Ozturk et al. 2014) and ω-3 polyunsaturated oils (Komaiko et al. 2016). Lecithins are used as
emulsifiers in many commercial nutritional and pharmaceutical products (Washington 1996). In
these applications, they are used to encapsulate nutrients, nutraceuticals, and drugs intended for
oral or intravenous delivery.
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2015). These molecules are typically either extracted from plant materials or produced by fer-
mentation using specific microorganisms (bacteria, yeasts, or fungi) (De et al. 2015, Uzoigwe
et al. 2015). In both cases, the biosurfactants typically have to be isolated from a complex mixture
of other molecules and then purified before they can be used as food ingredients.
Molecular and physicochemical characteristics. Biosurfactants have both hydrophilic and hy-
drophobic parts on the same molecule and can therefore adsorb to oil-water interfaces, reduce the
interfacial tension, and form a protective coating. Potential advantages of biosurfactants are that
they are natural, biodegradable, and sustainable and often have low toxicity (Kralova & Sjoblom
2009, Uzoigwe et al. 2015). Some examples of biosurfactants include glycolipids (sophorolipids,
rhamnolipids, and trehalose lipids) and lipopeptides (surfactin, iturin, and fengycin) (Kralova &
Sjoblom 2009, Uzoigwe et al. 2015).
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as well as their mixtures (Perfumo et al. 2010, Raikos et al. 2014). Bioemulsifiers are amphiphilic
biomolecules that can emulsify oil and water phases, but they are typically not as effective at re-
ducing the interfacial tension as biosurfactants because of their higher molecular weight (Uzoigwe
et al. 2015). Some examples of bioemulsifiers include hydrophobins, mannoproteins, emulsan, and
alasan (Araujo et al. 2014, Uzoigwe et al. 2015, Wosten & Scholtmeijer 2015). However, only a few
studies have investigated the potential use of bioemulsifiers in food systems, e.g., mannoproteins
(da Silva Araújo et al. 2014, Torabizadeh et al. 1996) and hydrophobins (Lumsdon et al. 2005,
Tchuenbou-Magaia et al. 2009).
In this section, only the properties of a select number of biosurfactants and bioemulsifiers that
may have potential application within the food industry are discussed: saponins, sophorolipids,
rhamnolipids, and mannoproteins (Table 1).
Saponins. The saponins are a broad class of natural surface-active molecules that have hydrophilic
regions (e.g., sugar groups) and hydrophobic regions (e.g., phenolic structures) on the same
molecule (Figure 4) (Mitra & Dungan 1997, Sidhu & Oakenfull 1986). Although they can be
isolated from different natural sources, the most commonly used saponins in the food industry
are extracted from the bark of the Quillaja saponaria tree. Indeed, a food emulsifier based on the
quillaja saponin extract is already sold under the trade name Q-Naturale R
for utilization in food
and beverage products (Ingredion, Bridgewater, NJ). This ingredient is provided in both pow-
dered and liquid forms that can be conveniently incorporated into foods. Quillaja saponins adsorb
to oil-water interfaces and reduce the interfacial tension, and are capable of forming and stabi-
lizing oil-in-water emulsions (Mitra & Dungan 1997; Waller & Yamasaki 1996a,b; Yang et al.
2013).
OH O O O O
O H
O O OH
HO H H HO
O O OH
O O
HO O O O O
OH O O O
HO OH O HO
HO O O O OH HO OH OH
HO
HO OH HO OH O O
HO
Quillaja saponin
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HO OH
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O
O
O HO O
HO O
O OH O
O O
O H
O OH O OH O
O H
O O HO HO O
O O
H
O
O OH HO HO HO
O H
OH OH OH
Sophorolipid Mono-rhamnolipid Di-rhamnolipid
Figure 4
Molecular structures of selected biosurfactants.
numbers of carbon atoms and degrees of unsaturation (Van Bogaert et al. 2011). In addition, the
carboxyl group at the end of the fatty acid chain can be either free or lactonized (form a ring struc-
ture with sophorose). In 2013, the production costs associated with synthesizing sophorolipids
by industrial fermentation processes were estimated to be approximately $2.54/kg (Ashby et al.
2013). Consequently, this type of emulsifier is relatively expensive and is likely to be utilized only
in niche applications.
Rhamnolipids. Rhamnolipids are another type of glycolipid that can be obtained from certain
microorganisms (e.g., Pseudomonas aeruginosa) using fermentation processes (Henkel et al. 2012,
Jirku et al. 2015, Muller et al. 2012). As with other biosurfactants, the microbial strain, fermentation
conditions, and substrates must be optimized. Rhamnolipids consist of one or two polar rhamnose
units attached to a nonpolar fatty acid chain containing a β-hydroxylalkanote (Figure 4) (Muller
et al. 2012, Saeedi et al. 2014). Rhamnolipids have a carboxylic acid group as part of the hydrophilic
regions and are therefore anionic biosurfactants under appropriate pH conditions. Rhamnolipids
can be synthesized using green chemistry approaches from natural materials, but the final product
is no longer natural. The advantage of chemically synthesizing them is that there is better control
over their final composition and functional properties.
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FO08CH11-McClements ARI 31 January 2017 9:55
in the cell walls of certain yeast strains (e.g., Saccharomyces cerevisiae or Saccharomyces uvarum).
Mannoproteins can be extracted from food-grade yeasts at a high yield using simple methods
(Alcantara et al. 2013, Barriga et al. 1999, Cameron et al. 1988, da Silva Araújo et al. 2014, Dikit
et al. 2010, Torabizadeh et al. 1996). Mannoproteins are glycoproteins consisting of mannose
chains (70–90%) covalently attached to a protein backbone (5–20%) (Barriga et al. 1999, Uzoigwe
et al. 2015).
Emulsion formation. Natural emulsifiers vary considerably in their ability to form emulsions.
The size of the droplets produced and the amount of emulsifier required to cover a given surface
area depend strongly on emulsifier type.
Saponins. Quillaja saponin is a highly effective emulsifier for fabricating oil-in-water emulsions
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containing small droplets (d < 200 nm) at low emulsifier-to-oil ratios (<1:10) (Ozturk et al. 2014,
Yang et al. 2013, Yang & McClements 2013). Typically, the saponin is dispersed in water at
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ambient temperature and then the oil and aqueous phases are homogenized. Quillaja saponins
have been used successfully to form stable emulsions from a variety of oils, including flavor oils
(Zhang et al. 2015a, 2016), omega-3 oils (Salminen et al. 2014, Uluata et al. 2015), medium-chain
triglycerides (Yang et al. 2013), vitamin D (Ozturk et al. 2015b), and vitamin E (Ozturk et al.
2014, Yang & McClements 2013).
Rhamnolipids. Rhamnolipids typically have HLB numbers ranging from low to intermediate,
i.e., approximately 4 to 8 (Torrego-Solana et al. 2014). They may therefore be most suitable
for stabilizing water-in-oil emulsions when used in isolation but may be useful for stabilizing
oil-in-water emulsions when used in conjunction with more hydrophilic emulsifiers or when
chemically modified. Rhamnolipids reduce the surface tension at an air-water interface from
approximately 72 mN/m to below 30 mN/m and have a critical micelle concentration (CMC)
of approximately 10–200 mg/L (Costa et al. 2010, Muller et al. 2012, Torrego-Solana et al.
2014). As with other biosurfactants produced by fermentation, their structure and functional
performance depends on microbial strain, fermentation conditions, and substrates used. There are
few publications on the formation of food-grade emulsions using rhamnolipids. Some studies have
shown they can be used to form essential oil-in-water emulsions (Nitschke et al. 2010, Sifour et al.
2007). A recent study showed that rhamnolipids could be used to form oil-in-water nanoemulsions
containing small stable droplets using microfluidization (Bai & McClements 2016).
Mannoproteins. Mannoproteins have been reported to be good emulsifiers because of the pres-
ence of hydrophilic mannose chains and a hydrophobic protein backbone (Barriga et al. 1999,
Cameron et al. 1988). The emulsifying and stabilizing activities of mannoproteins have been re-
lated to the amino acid composition and high molecular weight (>50 kDa) of the protein fraction
(da Silva Araújo et al. 2014). The hydrophobic protein helps anchor the mannoproteins to the oil
droplet surfaces, whereas the hydrophilic mannose chains give stability through steric repulsion
(Barriga et al. 1999). Mannoproteins have been shown to have similar or better emulsification ac-
tivity than other natural emulsifiers, such as gum arabic and lecithin (Dikit et al. 2010) or sodium
caseinate (Torabizadeh et al. 1996).
Emulsion stability. Natural emulsifiers also vary considerably in their ability to stabilize emul-
sions against environmental stresses, which is due to differences in the nature of the interfacial
coatings they form around droplets, e.g., charge, thickness, polarity, and reactivity.
Saponins. The major stabilization mechanism for oil droplets coated by quillaja saponins appears
to be a combination of electrostatic and steric repulsion. Quillaja saponin is capable of forming
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oil-in-water emulsions that are stable over a range of pH values, ionic strengths, and temperatures
(Ozturk et al. 2014, Yang et al. 2013, Yang & McClements 2013). In the absence of salt, saponin-
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coated oil droplets had good aggregation stability from pH 8 to pH 3 because of a high negative
charge that generated a strong electrostatic repulsion (Figure 3a). However, they flocculated
at pH 2 because of a reduction in their negative charge and therefore electrostatic repulsion
(Figure 3b). Interestingly, the emulsions were stable to droplet coalescence at these highly
acidic conditions, which suggests that the interfacial layer was resistant to disruption when
the droplets were in close contact. At neutral pH, saponin-coated oil droplets are unstable to
droplet aggregation when the salt concentration exceeded a particular level (≥400-mM NaCl)
because of electrostatic screening. Saponin-coated oil droplets have good thermal stability (30
to 90◦ C, 30 min, no salt, pH 7) because of the strong electrostatic and steric repulsion between
them. Quillaja saponins can also protect oil droplets from aggregation when the lipid phase
crystallizes, which is important for preventing partial coalescence and for the production of solid
lipid nanoparticles (Salminen et al. 2014).
Sophorolipids. There have been few studies of the factors influencing the stability of sophorolipid-
coated oil droplets. One study reported that emulsions stored at pH 7.0 or pH 7.2 were more stable
to droplet aggregation than those stored at pH 5.8 (Xue et al. 2013). Droplet aggregation at the
lower pH may have occurred because of a reduction in electrostatic repulsion between the droplets
when their negative charge was reduced under acidic conditions. Another study reported that
coarse emulsions formed by vortexing had relatively good stability (Daverey & Pakshirajan 2010).
However, the methods used to test emulsions did not provide any details about the instability
mechanism or about the factors influencing stability.
Mannoproteins. Only a few studies have examined the potential use of mannoproteins as emulsi-
fiers in food systems. Moreover, most of these studies fabricated the emulsions using simple mixing
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or vortexing methods, and thus are not representative of actual food applications. Nonetheless,
it has been reported that mannoprotein-stabilized emulsions were stable to a wide range of pH
values (pH 3 to pH 11) and up to 5% sodium chloride (Dikit et al. 2010, Torabizadeh et al. 1996).
Applications. Saponins have been used as emulsifiers to form and stabilize emulsion-based deliv-
ery systems for vitamin E (Ozturk et al. 2014, Yang & McClements 2013), vitamin D (Ozturk et al.
2015b), and ω-3 oils (Salminen et al. 2014, Uluata et al. 2015). As mentioned earlier, saponin-
based emulsifiers (Q-Naturale R
) are commercially available and are already being used in many
commercial food applications. Sophorolipids have been used to encapsulate structured lipids (in-
teresterified soybean and rice bran oils) in oil-in-water emulsions (Xue et al. 2013). Rhamnolipids
have been used to form oil-in-water emulsions containing antimicrobial essential oils (Haba et al.
2014) and triglyceride oils (Bai & McClements 2016). Surfactin has been used to fabricate oil-
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in-water nanoemulsions using sunflower oil ( Joe et al. 2012). Mannoproteins have been tested
as emulsifiers in salad dressing (Dikit et al. 2010) and mayonnaise (da Silva Araújo et al. 2014,
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Torabizadeh et al. 1996). Hydrophobins have been patented by Unilever for their potential ap-
plication in a variety of emulsion-based food products (Cox & Kim 2013).
Proteins
Many food proteins are amphiphilic molecules capable of adsorbing to oil droplet surfaces and
stabilizing them against aggregation, e.g., those derived from animals, plants, insects, and mi-
croorganisms (Lam & Nickerson 2013).
Molecular and physicochemical characteristics. The number of exposed polar and nonpolar
groups on the surfaces of proteins governs their water solubility and surface activity: Too many
nonpolar groups leads to poor water solubility, whereas too few nonpolar groups leads to low
surface activity. As a result, an optimum level of nonpolar and polar surface groups is required to
ensure optimum water solubility and surface activity.
Food proteins have different types, numbers, and sequences of anionic, neutral, and
cationic amino acids along their polypeptide chains, which determine their electrical proper-
ties (Damodaran et al. 2007). The electrical properties of proteins are conveniently characterized
by their ζ-potential versus pH profiles. Typically, the ζ-potential goes from negative at high
pH, to zero at intermediate pH (the isoelectric point, or pI), to positive at low pH (Figure 3a).
The electrical properties of proteins play an important role in determining the properties of
protein-stabilized emulsions, such as their physical or chemical stability (Lam & Nickerson 2013,
McClements 2015a), and their ability to interact with other charged substances, such as other
proteins or polysaccharides (Kayitmazer et al. 2013, Kizilay et al. 2011).
The three-dimensional structure of free or adsorbed proteins depends on the balance of van
der Waals forces, hydrogen bonding, hydrophobic interactions, electrostatic interactions, cova-
lent bonds, and conformational entropy effects (Lam & Nickerson 2013, Nishinari et al. 2014).
As a result, protein structure is particularly sensitive to solution and environmental conditions,
such as pH, ionic strength, and temperature. In general, the three-dimensional structures adopted
by surface-active proteins can be classified as globular or random coil (Dickinson 2003). Glob-
ular proteins have compact spheroid structures with most of the nonpolar groups tucked into
the interior and most of the polar groups at the exterior (Tcholakova et al. 2008). However,
owing to conformational constraints, most globular proteins still have some nonpolar groups
located at their exteriors, which generate a thermodynamic driving force for their adsorption to
oil-water interfaces due to the hydrophobic effect (Norde 2011). There are numerous examples of
Water – – –
–
–
Oil
Saponins Polysaccharides
– – – – – –
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– – – – – –
Globular proteins
Figure 5
Schematic representation of different kinds of natural food-grade emulsifiers that may be used in the food industry. (a) Surface-active
lipids, such as saponins and phospholipids, have a polar head group and a nonpolar tail group. (b) Surface-active biopolymers, such as
proteins and polysaccharides, have nonpolar and polar regions on the same macromolecule.
surface-active globular proteins that can be used as emulsifiers in the food industry, such as those
derived from animals, fish, milk, eggs, plants, and microorganisms (Table 1). Random coil proteins
(such as casein and gelatin) have more flexible conformations, although they may still have some
regions containing secondary structure, such as α-helix or β-sheet. Protein conformation often
changes after they adsorb to oil droplet surfaces because the change in their local environment
alters the balance between molecular interactions and entropy effects (Norde 2011). Globular
protein unfolding at oil droplet surfaces leads to exposure of nonpolar and sulfhydryl groups nor-
mally tucked into the protein interior (McClements et al. 1993, Monahan et al. 1993, Wierenga
et al. 2006). As a result, the reactivity of the globular proteins increases because they can now form
hydrophobic or disulfide bonds with other protein molecules on similar or different droplets. Ad-
sorbed proteins tend to adopt a conformation in which the majority of polar groups protrude into
the water phase, whereas the majority of nonpolar groups protrude into the oil phase (Figure 5).
At present, proteins derived from bovine milk (whey proteins and caseins) are the most com-
monly used as food emulsifiers (Wilde 2009), although other types of animal-based proteins are
commonly used in some food products, such as fish, meat, and egg proteins (Lam & Nickerson
2013). For example, egg proteins are widely used in mayonnaise, whereas meat proteins are widely
used in meat products such as sausages. Recently, there has been interest in the development of
sustainably produced foods that are suitable for individuals with specialist dietary requirements
(such as vegan, vegetarian, or Kosher). As a result, there has been considerable research on iden-
tifying, extracting, and characterizing surface-active proteins from plant-based sources, such as
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canola, chickpea, legume, lentil, pea, wheat, maize, lupin, sorghum, and soy proteins (Day 2013,
Karaca et al. 2015, Lam & Nickerson 2013). Some examples of food proteins that are currently
utilized as emulsifiers or that have potential for being utilized are highlighted in Table 1.
Emulsion formation. The ability of a protein to form small droplets during homogenization
depends on its molecular characteristics, such as molar mass, polarity, and charge (Karaca et al.
2015, Lam & Nickerson 2013, McClements 2015a). These molecular characteristics depend on
the source of the protein, as well as on the conditions used to extract, purify, and store it. Proteins
that are too hydrophilic are not particularly effective emulsifiers because they do not strongly
adsorb to oil droplet surfaces, e.g., some forms of gelatin (Gomez-Guillen et al. 2011). However,
proteins that are too hydrophobic, e.g., zein and gliadin, tend to aggregate with each other,
thereby reducing their water solubility and surface activity (Luo & Wang 2014). Proteins that
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are good emulsifiers must therefore have a balance of hydrophilic and hydrophobic groups that
allows them to be soluble in water but also surface active. Even so, there are still considerable
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differences in the ability of proteins to form emulsions because of differences in their adsorption
kinetics, surface loads, saturation surface pressures, interfacial thicknesses, surface hydrophobicity,
and electrical properties (Wierenga et al. 2006). Numerous studies have shown that stable oil-
in-water emulsions containing relatively small droplets (d < 300 nm) can be formed using food
proteins, such as whey, casein, soy, gelatin, pea, and legume proteins (Benjamin et al. 2014, Donsı̀
et al. 2010, Liang et al. 2016, Maher et al. 2011, Zhang et al. 2015b). Typically, the surface load
of food proteins is approximately 1 to 10 mg/m2 , depending on their molecular characteristics
and solution conditions, such as pH, ionic strength, temperature, and total protein concentration
(Table 1).
Proteins from animal origin, particularly from milk (casein and whey protein) and eggs (ovalbu-
min and lysozyme), have been widely used as emulsifiers but with differences in their emulsification
properties. For example, both β-lactoglobulin and lactoferrin can be used to produce emulsions
containing small fat droplets (d32 = 0.14 μm), but the amount of protein required to achieve this
size was considerably different (Mao & McClements 2011). Much less β-lactoglobulin was needed
because it has a lower molecular weight and may therefore adsorb more rapidly and form thinner
layers (Mao & McClements 2011). Moreover, these two proteins have different electrical charge
versus pH profile because of their different isoelectric points (pI), with β-lactoglobulin having a
pI around pH 5 and lactoferrin around pH 8 (Mao & McClements 2011). Caseins have also been
widely used as emulsifiers in the food industry (Cerimedo et al. 2010, Liang et al. 2014, Srinivasan
et al. 2002). Sodium caseinates, which consist of four different protein fractions, αs1 -, αs2 -, β-,
and κ-caseins, are highly effective emulsifiers. They have been reported to have a surface load that
increases (from 0.5 to 3 mg/m2 ) with increasing protein-to-oil ratio (Srinivasan et al. 2002), which
may be due to the formation of multiple layers of casein at the droplet surfaces.
Plant proteins typically form thicker interfacial layers than dairy proteins (Day 2013), which
may be due to their larger molecular dimensions (Wong et al. 2012). Soy protein is one of the plant-
based proteins that have been most extensively studied for its emulsifying properties (Day 2013).
The two major proteins in soybeans are glycinin and β-conglycinin (Keerati-u-rai & Corredig
2009, 2010). Both proteins form interfacial layers approximately 30–40 nm thick around oil sur-
faces (Keerati-u-rai & Corredig 2010). β-Conglycinin has been reported to have better emulsifying
properties than soy protein isolate and glycinin because of its smaller molecular mass, higher flex-
ibility, and larger hydrophobicity (Keerati-u-rai & Corredig 2010, Molina et al. 2001). Both
β-conglycinin and glycinin are highly sensitive to heat treatment because of changes in
conformation, aggregation state, and surface reactivity (Keerati-u-rai & Corredig 2009). Soy
protein isolates, which contain a mixture of β-conglycinin and glycinin, have also been used to
35 25
a + b
Fava bean Fava bean
15 + +
ζ-potential (mV)
15
5 pI
10
–5 –
–
– 5 –
–15
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–25 0
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2 3 4 5 6 7 8 9 2 3 4 5 6 7 8 9
pH pH
Figure 6
Change in (a) droplet charge (ζ-potential) and (b) mean particle diameter with pH for emulsions containing droplets coated by
plant-based protein emulsifiers: fava bean, lentil, and pea protein. Here, pI is the isoelectric point of the protein-coated droplets, i.e.,
point of zero charge.
form stable oil-in-water emulsions (Fernandez-Avila et al. 2015, Keerati-u-rai & Corredig 2009).
A recent study showed that relatively small emulsion droplets (d3,2 < 0.4 μm) could be formed
using plant protein isolates (soy, pea, and lupin) (Benjamin et al. 2014).
Emulsion stability. The interfacial coatings formed around oil droplets by protein molecules are
typically fairly thin (1 to 10 nm), which means that the range of the steric repulsion is relatively
short compared with the range of the van der Waals attraction (Dickinson 2003, Lam & Nickerson
2013, McClements 2004). As a result, protein-coated droplets tend to aggregate in the absence
of other strong repulsive interactions. The most common additional repulsive interaction is the
electrostatic repulsion that arises due to the electrical charge on the adsorbed proteins (Figure 3a).
The magnitude and range of this electrostatic repulsion depends on the surface charge density
of the protein-coated droplets and the ionic strength of the surrounding aqueous phase. The
electrostatic repulsion tends to decrease when the droplet charge decreases and when the ionic
strength increases. As a result, the stability of protein-coated droplets is highly dependent on pH
and salt addition (Figure 3b).
A typical example of the impact of pH on emulsion stability is highlighted in Figure 6 for
emulsions containing plant protein–coated oil droplets. These plant proteins are all globular
proteins that form relatively thin interfacial layers. At pH values sufficiently above or below the
proteins’ isoelectric points, the emulsions are stable to flocculation because they have a high
negative or positive charge, respectively. However, at pH values around the isoelectric point the
droplets are highly susceptible to flocculation and creaming because they have little net charge.
Nevertheless, the protein-coated oil droplets may still be relatively stable to coalescence because
of the strong short-range steric repulsion associated with the protein layer. This type of pH
sensitivity is observed for a wide range of food-grade protein emulsifiers and is one of their major
drawbacks for certain food applications.
Another important type of colloidal interaction in emulsions stabilized by globular proteins is
the hydrophobic attraction. Globular proteins may undergo conformational changes (surface or
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Increased surface
hydrophobicity
102
Thermal
Particle diameter (μm)
denaturation
101
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100
30 40 50 60 70 80 90 100
Temperature (°C)
Figure 7
Droplet aggregation may occur in globular-protein stabilized emulsions when they are heated above their
thermal denaturation temperature because of an increase in surface hydrophobicity. This figure shows the
change in particle size of β-lactoglobulin-stabilized emulsions containing 150-mM NaCl added before
heating.
thermal denaturation) after adsorption to oil droplet surfaces, which leads to exposure of nonpolar
groups. The resulting increase in surface hydrophobicity leads to the generation of a relatively
strong hydrophobic attraction between the droplets. This attractive force causes droplet aggrega-
tion if it is stronger than the repulsive forces, e.g., electrostatic repulsion, in the system. Moreover,
amino acids containing disulfide or sulfhydryl groups may be exposed after protein denaturation,
which can lead to the formation of covalent linkages between proteins adsorbed on similar or
different droplets (Kim et al. 2002a,b). An example of the influence of hydrophobic interactions
on the stability of whey protein–stabilized emulsions is shown in Figure 7. There is a substantial
increase in droplet aggregation when emulsions containing 150-mM NaCl were heated above
approximately 60◦ C, which can be attributed to thermal denaturation of the adsorbed proteins. In
the absence of salt, no droplet aggregation was observed because there was a strong electrostatic
repulsion between the droplets that stopped them from aggregating, even after protein denatu-
ration. In the presence of salt, the electrostatic interactions between the droplets were screened;
thus, when the globular proteins unfolded, the hydrophobic attraction was large enough to over-
come the electrostatic repulsion. Similar behaviors have been observed for other globular proteins,
including pea, legume, and lactoferrin (Can Karaca et al. 2011, Gharsallaoui et al. 2010, Tokle &
McClements 2011). Casein-coated droplets do not exhibit this kind of heat instability because
they are flexible proteins rather than globular proteins.
Protein emulsifiers may also improve the chemical stability of oil-in-water emulsions. For
example, some proteins form coatings that inhibit lipid oxidation in emulsions (Berton et al. 2011,
Kargar et al. 2011, Nielsen et al. 2013). The ability of adsorbed proteins to inhibit oxidation
may be attributed to various physicochemical mechanisms, such as free radical scavenging, iron
chelation, steric hindrance, and electrostatic repulsion (Waraho et al. 2011).
Applications. Certain types of proteins are already widely used in the food industry to form
and stabilize emulsion-based food products, such as beverages, sauces, dressings, and desserts.
In particular, proteins derived from bovine milk (such as casein and whey proteins) are sold
commercially as emulsifiers for use in foods and beverages (Lam & Nickerson 2013, Wilde 2009).
Whey protein ingredients contain a mixture of globular proteins, whereas caseins contain a mixture
of random coil proteins. Commercial casein and whey protein ingredients typically have good water
dispersibility, surface-activity, and emulsion-stabilizing properties when used under appropriate
conditions (pH, ionic strength, and temperature). Egg yolk and white both contain a mixture of
globular proteins that can act as good emulsifiers under suitable conditions and are widely used in
some emulsion-based food products (Anton 2013, Lam & Nickerson 2013). Again, these proteins
can be purchased commercially as functional ingredients for application in the food industry.
Flexible proteins derived from animals or fish, such as gelatin, may also be used as emulsifiers in
Annu. Rev. Food Sci. Technol. 2017.8:205-236. Downloaded from www.annualreviews.org
been reported, including chickpeas, corn, lentils, peas, lupins, and soybeans (Benjamin et al. 2014,
Keerati-u-rai & Corredig 2009, Lam & Nickerson 2013). Most of these are globular proteins
whose functionality is highly dependent on any changes in their structure during the isolation
process. Some plant-based proteins have good potential as natural emulsifiers, but in other cases
they have to be modified (physically, chemically, or enzymatically) before they function effectively.
Polysaccharides
A number of natural or chemically modified polysaccharides can be used to form and stabilize
emulsions because they contain both polar and nonpolar groups on the same molecule, such as
gum arabic, beet pectin, and modified starch.
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Schmidt et al. 2015a,b). The emulsifying properties of pectins have been attributed to the presence
of a hydrophobic protein or phenolic fraction that promotes adsorption to oil droplet surfaces, and
a hydrophilic polysaccharide fraction that provides good steric stabilization. Amphiphilic polysac-
charides isolated from corn by-products (corn fiber gum) are also capable of forming and stabilizing
oil-in-water emulsions (Yadav et al. 2008, 2009). The surface activity of corn fiber gum has been
attributed to the presence of a hydrophilic polysaccharide backbone with hydrophobic polypep-
tide and/or phenolic groups attached. Other polysaccharides capable of forming and stabilizing
emulsions have also been studied, including those from yellow mustard mucilage (Wu et al. 2015),
chitosan (Klinkesorn 2013), soybeans (Chivero et al. 2014), basil seeds (Osano et al. 2014), gum
tragacanth (Farzi et al. 2013), and olives (Filotheou et al. 2015). Nevertheless, additional research
is required to establish their potential commercial application, including establishing their pro-
duction economics, batch-to-batch variations, reliability of source, and functional performance.
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Emulsion formation. Amphiphilic polysaccharides are typically relatively large molecules that
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form thick interfacial layers after they adsorb to oil droplet surfaces. Consequently, a relatively high
amount of emulsifier is adsorbed per unit surface area at saturation (high surface load). One of the
consequences of this attribute is that relatively high levels of polysaccharides are typically required
to generate small droplets during homogenization (Figure 2). The mass ratio of emulsifier-to-oil
required to form an emulsion with a given droplet diameter (d32 ) is given by
mE 6·
= . 2.
mO ρO d 32
Here, is the surface load and ρ 0 is the density of the oil phase. Recent studies in our laboratory
found that the surface load of gum arabic was approximately 64 mg/m2 , but that of whey protein
was approximately 2 mg/m2 . Thus, to produce oil droplets with a mean diameter of approximately
300 nm would require an emulsifier-to-oil ratio of approximately 1.4:1 for gum arabic and 0.043:1
for whey protein. This issue is important for other amphiphilic polysaccharides with high molecu-
lar weights and surface loads. However, recent studies have shown that certain processing methods
(such as controlled heating) can decrease the amounts of amphiphilic polysaccharides (e.g., gum
arabic) required to form emulsions (Wu et al. 2015).
The effectiveness of polysaccharides at forming emulsions may also be influenced by their
adsorption kinetics and ability to reduce interfacial tensions. Polysaccharides tend to adsorb rela-
tively slowly to the oil droplet surfaces during homogenization, which may lead to some droplet
coalescence within the homogenizer. In addition, polysaccharides are often not as effective as
other types of emulsifiers at reducing the interfacial tension, and therefore the Laplace pressure
of the droplets is relatively high, which means that small droplets may not be generated dur-
ing homogenization. For example, the interfacial tension of gum arabic has been reported to be
around 10 mJ/m2 for an oil-water interface (Huang et al. 2001), which is considerably higher than
the values of 8 and 5mJ/m2 reported for proteins (Chang et al. 2015) and biosurfactants (Hunter
2001), respectively.
Emulsion stability. Polysaccharides form relatively thick hydrophilic coatings around oil
droplets and therefore generate strong long-range steric repulsion (McClements 2015a). Con-
sequently, polysaccharide-coated droplets tend to be much less affected by changes in pH and
ionic strength than protein-coated droplets, which are mainly stabilized by electrostatic repulsion
(Figure 3b). Having said this, many polysaccharides do have ionizable groups that can contribute
an electrical charge to droplet surfaces (Figure 3a). This electrical charge may be important for
certain applications of polysaccharide emulsifiers. For example, they may influence the ability of
electrically charged species to interact with the oil droplet surfaces, such as mineral ions, ionic
surfactants, proteins, or other polysaccharides. In addition, the electrical charge of polysaccharides
is important for the fabrication of some structured emulsions, such as multilayer emulsions and
filled hydrogels (McClements 2012).
Studies have demonstrated the good pH and salt stability of polysaccharide-coated oil droplets.
For example, gum arabic–coated droplets are stable to droplet aggregation over a wide range of
pH (pH 3 to pH 9) and ionic strengths (0–500-mM NaCl and 0–25-mM CaCl2 ) (Chanamai &
McClements 2002, Charoen et al. 2011, Ozturk et al. 2015a, Qian et al. 2011). Gum arabic–coated
oil droplets have also been reported to be stable to elevated temperatures (up to 90◦ C) because of
strong steric repulsion (Charoen et al. 2011). Similar results have been reported for other kinds
of polysaccharide emulsifiers (Zeeb et al. 2011).
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Applications. Certain types of polysaccharides are already widely used as emulsifiers in the food
industry. Gum arabic and modified starch are commonly employed in the beverage industry to
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create soft drinks (Piorkowski & McClements 2014). In these applications, they are typically used
to encapsulate flavor oils (flavor emulsions) or triglyceride oils (cloud emulsions). Polysaccharide
emulsifiers tend to be less useful for application in products with high fat contents (such as dress-
ings, dips, or sauces) because the emulsifier-to-oil ratio required is too high. A major advantage
of this type of emulsifier is that it tends to produce oil droplets that are highly stable to changes in
pH, ionic strength, or temperature. However, the droplets produced during homogenization are
often quite large because polysaccharides adsorb relatively slowly and are not particularly effective
at reducing the interfacial tension, and high levels of emulsifier are required because of their high
surface loads.
Co-adsorption. Two or more natural emulsifiers are employed in the same system to form mixed
interfacial coatings around oil droplets (Dickinson 2011, Pugnaloni et al. 2004). Mixed interfacial
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Hydrophilic pickering:
Colloidal particles with
different wettability at
oil-water interfaces
Oil phase
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θ θ
θ θ θ = 90°
Aqueous phase
Increasing water wettability of particles
Figure 8
Emulsion droplets can be stabilized by small particles that adsorb to the droplet surfaces. Oil droplets can be
stabilized by small particles that protrude into the aqueous phase, whereas water droplets can be stabilized by
small particles that protrude into the oil phase.
coatings can be formed by including both emulsifiers in the system before homogenization. Alter-
natively, one type of natural emulsifier can be added to the system before homogenization, whereas
the other is added after homogenization. The composition and structure of the mixed coatings
depend on the surface activities, concentrations, and order of the addition of the two emulsifiers.
the oil droplet surfaces because of electrostatic attraction. This process can be repeated numerous
times using polyelectrolytes with different charges to form nanolaminated coatings.
Source
The source of a natural emulsifier should be abundant, inexpensive, and reliable. In addition, the
process used to isolate the emulsifiers from this source should be relatively facile, reproducible,
and economically viable. A major problem with many natural emulsifiers is that their composition
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and functionality vary widely from batch to batch depending on variations in their origin and
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isolation procedures.
Economics
To be commercially viable, natural emulsifiers must have a price that is competitive with synthetic
surfactants. Consequently, the economics of isolating, purifying, and preparing food ingredients
from natural emulsifiers must be carefully considered. Natural emulsifiers are often isolated from
sources that are waste streams from other food processing operations, which makes them more
economically viable. For example, whey proteins are by-products of cheese that are converted
into value-added ingredients. The relatively high cost of producing biosurfactants by microbial
fermentation can be partly offset by using protein-, carbohydrate-, and lipid-rich waste products
from other processes, such as those used in the dairy, vegetable, meat, sugar, or oil industries (De
et al. 2015).
Functional Attributes
Another important factor to consider is the functional performance of the ingredient in food
applications. Ideally, the emulsifier should be capable of forming relatively small droplets that are
stable over a wide range of conditions (such as pH, ionic strength, and temperature variations).
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problem. However, newly developed biosurfactants may require government approval before they
can be used within foods, which may be expensive and time consuming.
differ in their costs, reliability of supply, consistency of performance, ease of utilization, and label
friendliness. Further research is required to identify new sources of commercially viable natural
Access provided by University of Melbourne on 02/24/20. For personal use only.
emulsifiers and to carefully and systematically characterize and compare their ability to form and
stabilize emulsions.
DISCLOSURE STATEMENT
The authors are not aware of any affiliations, memberships, funding, or financial holdings that
might be perceived as affecting the objectivity of this review.
ACKNOWLEDGMENTS
This material was partly based on work supported by the Cooperative State Research, Extension,
and Education Service, USDA, Massachusetts Agricultural Experiment Station (MAS00491), as
well as by a USDA NRI Grant (2013–03795). We also thank Nestle and DSM for providing funds
that partly supported this research.
LITERATURE CITED
Alba K, Ritzoulis C, Georgiadis N, Kontogiorgos V. 2013. Okra extracts as emulsifiers for acidic emulsions.
Food Res. Int. 54:1730–37
Alcantara VA, Pajares IG, Simbahan JF, Edding SN. 2013. Downstream recovery and purification of a bioemul-
sifier from Saccharomyces cerevisiae 2031. Philipp. Agric. Sci. 96:349–58
Ali A, Mekhloufi G, Huang N, Agnely F. 2016. β-lactoglobulin stabilized nanoemulsions: formulation and
process factors affecting droplet size and nanoemulsion stability. Int. J. Pharm. 500:291–304
Anton M. 2013. Egg yolk: structures, functionalities and processes. J. Sci. Food Agric. 93:2871–80
Araujo VBD, de Melo ANF, Costa AG, Castro-Gomez RH, Madruga MS, et al. 2014. Followed extraction
of β-glucan and mannoprotein from spent brewer’s yeast (Saccharomyces uvarum) and application of the
obtained mannoprotein as a stabilizer in mayonnaise. Innov. Food Sci. Emerg. Technol. 23:164–70
Ashby RD, McAloon AJ, Solaiman DKY, Yee WC, Reed M. 2013. A process model for approximating the
production costs of the fermentative synthesis of sophorolipids. J. Surfactants Deterg. 16:683–91
Bai L, McClements DJ. 2016. Formation and stabilization of nanoemulsions using biosurfactants: rhamno-
lipids. J. Colloid Interface Sci. 479:71–79
Baines D, Seal R. 2012. Natural Food Additives, Ingredients and Flavourings. Cambridge, UK: Woodhead Publ.
Barriga JA, Cooper DG, Idziak ES, Cameron DR. 1999. Components of the bioemulsifier from S. cerevisiae.
Enzyme Microb. Technol. 25:96–102
Bellesi FA, Martinez MJ, Ruiz-Henestrosa VMP, Pilosof AM. 2016. Comparative behavior of protein or
polysaccharide stabilized emulsion under in vitro gastrointestinal conditions. Food Hydrocoll. 52:47–56
Benjamin O, Silcock P, Beauchamp J, Buettner A, Everett DW. 2014. Emulsifying properties of legume
proteins compared to β-lactoglobulin and Tween 20 and the volatile release from oil-in-water emulsions.
J. Food Sci. 79:E2014–22
Berton C, Ropers M-H, Viau M, Genot C. 2011. Contribution of the interfacial layer to the protection of
emulsified lipids against oxidation. J. Agric. Food Chem. 59:5052–61
Berton-Carabin CC, Schroën K. 2015. Pickering emulsions for food applications: background, trends, and
challenges. Annu. Rev. Food Sci. Technol. 6:263–97
Bueschelberger HG. 2004. Lecithins. In Emulsifiers in Food Technology, ed. RJ Whitehurst, pp. 1–39. Oxford,
UK: Blackwell Publ.
Cabezas DM, Diehl BW, Tomás MC. 2015. Emulsifying properties of hydrolysed and low HLB sunflower
lecithin mixtures. Eur. J. Lipid Sci. Technol. 117:975–83
Cabezas DM, Madoery R, Diehl BWK, Tomas MC. 2012. Emulsifying properties of different modified
sunflower lecithins. J. Am. Oil Chem. Soc. 89:355–61
Annu. Rev. Food Sci. Technol. 2017.8:205-236. Downloaded from www.annualreviews.org
Cameron DR, Cooper DG, Neufeld R. 1988. The mannoprotein of Saccharomyces cerevisiae is an effective
bioemulsifier. Appl. Environ. Microbiol. 54:1420–25
Access provided by University of Melbourne on 02/24/20. For personal use only.
Can Karaca A, Nickerson MT, Low NH. 2011. Lentil and chickpea protein-stabilized emulsions: optimization
of emulsion formulation. J. Agric. Food Chem. 59:13203–11
Casado V, Martin D, Torres C, Reglero G. 2012. Phospholipases in food industry: a review. Lipases Phospho-
lipases Methods Protoc. 861:495–523
Cerimedo MSÁ, Iriart CH, Candal RJ, Herrera ML. 2010. Stability of emulsions formulated with high
concentrations of sodium caseinate and trehalose. Food Res. Int. 43:1482–93
Chanamai R, McClements DJ. 2002. Comparison of gum arabic, modified starch, and whey protein isolate as
emulsifiers: influence of pH, CaCl2 and temperature. J. Food Sci. 67:120–25
Chang C, Niu F, Su Y, Qiu Y, Gu L, Yang Y. 2016. Characteristics and emulsifying properties of acid and
acid-heat induced egg white protein. Food Hydrocoll. 54:342–50
Chang C, Tu S, Ghosh S, Nickerson M. 2015. Effect of pH on the inter-relationships between the physico-
chemical, interfacial and emulsifying properties for pea, soy, lentil and canola protein isolates. Food Res.
Int. 77:360–67
Charoen R, Jangchud A, Jangchud K, Harnsilawat T, Naivikul O, McClements DJ. 2011. Influence of biopoly-
mer emulsifier type on formation and stability of rice bran oil-in-water emulsions: whey protein, gum
arabic, and modified starch. J. Food Sci. 76:E165–72
Chivero P, Gohtani S, Yoshii H, Nakamura A. 2014. Physical properties of oil-in-water emulsions as a function
of oil and soy soluble polysaccharide types. Food Hydrocoll. 39:34–40
Choe J, Oh B, Choe E. 2014. Effect of soybean lecithin on iron-catalyzed or chlorophyll-photosensitized
oxidation of canola oil emulsion. J. Food Sci. 79:C2203–C08
Choi SJ, Decker EA, Henson L, Popplewell LM, Xiao H, McClements DJ. 2011. Formulation and properties
of model beverage emulsions stabilized by sucrose monopalmitate: influence of pH and lyso-lecithin
addition. Food Res. Int. 44:3006–12
Costa S, Nitschke M, Lepine F, Deziel E, Contiero J. 2010. Structure, properties and applications of rham-
nolipids produced by Pseudomonas aeruginosa L2-1 from cassava wastewater. Process Biochem. 45:1511–16
Cox AR, Kim H. 2013. Oil-in-water emulsion. Patent No. WO2010136355-A1
Damodaran S, Parkin KL, Fennema OR. 2007. Fennema’s Food Chemistry. Boca Raton, FL: CRC Press
da Silva Araújo VB, de Melo ANF, Costa AG, Castro-Gomez RH, Madruga MS, et al. 2014. Followed extrac-
tion of β-glucan and mannoprotein from spent brewer’s yeast (Saccharomyces uvarum) and application of
the obtained mannoprotein as a stabilizer in mayonnaise. Innov. Food Sci. Emerg. Technol. 23:164–70
Daverey A, Pakshirajan K. 2010. Sophorolipids from Candida bombicola using mixed hydrophilic substrates:
production, purification and characterization. Colloids Surf. B 79:246–53
Day L. 2013. Proteins from land plants: potential resources for human nutrition and food security. Trends
Food Sci. Technol. 32:25–42
De S, Malik S, Ghosh A, Saha R, Saha B. 2015. A review on natural surfactants. RSC Adv. 5:65757–67
Deepika K, Kalam S, Sridhar PR, Podile AR, Bramhachari P. 2016. Optimization of rhamnolipid biosurfactant
production by mangrove sediment bacterium Pseudomonas aeruginosa KVD-HR42 using response surface
methodology. Biocatal. Agric. Biotechnol. 5:38–47
230 McClements · ·
Bai Chung
FO08CH11-McClements ARI 31 January 2017 9:55
de Folter JWJ, van Ruijven MWM, Velikov KP. 2012. Oil-in-water Pickering emulsions stabilized by colloidal
particles from the water-insoluble protein zein. Soft Matter 8:6807–15
de Oliveira MR, Magri A, Baldo C, Camilios-Neto D, Minucelli T, Pedrine Colabone Celligoi MA. 2015.
Review: sophorolipids a promising biosurfactant and its applications. Int. J. Adv. Biotechnol. Res. 16:161–74
Dickinson E. 2003. Hydrocolloids at interfaces and the influence on the properties of dispersed systems. Food
Hydrocoll. 17:25–39
Dickinson E. 2011. Mixed biopolymers at interfaces: competitive adsorption and multilayer structures. Food
Hydrocoll. 25:1966–83
Dickinson E. 2012. Use of nanoparticles and microparticles in the formation and stabilization of food emul-
sions. Trends Food Sci. Technol. 24:4–12
Dickinson E, Rolfe SE, Dalgleish DG. 1988. Competitive adsorption of αs1 -casein and β-casein in oil-in-water
emulsions. Food Hydrocoll. 2:397–405
Dikit P, Maneerat S, Musikasang H, H-Kittikun A. 2010. Emulsifier properties of the mannoprotein extract
Annu. Rev. Food Sci. Technol. 2017.8:205-236. Downloaded from www.annualreviews.org
Haba E, Bouhdid S, Torrego-Solana N, Marques AM, Espuny MJ, et al. 2014. Rhamnolipids as emulsifying
agents for essential oil formulations: antimicrobial effect against Candida albicans and methicillin-resistant
Staphylococcus aureus. Int. J. Pharm. 476:134–41
Hasenhuettl GL. 2008. Overview of food emulsifiers. In Food Emulsifiers and Their Applications, ed. GL
Hasenhuettl, RW Hartel, pp. 1–9. New York: Springer-Verlag
Henkel M, Muller MM, Kugler JH, Lovaglio RB, Contiero J, et al. 2012. Rhamnolipids as biosurfactants from
renewable resources: concepts for next-generation rhamnolipid production. Process Biochem. 47:1207–19
Heo W, Kim JH, Pan JH, Kim YJ. 2016. Lecithin-based nano-emulsification improves the bioavailability of
conjugated linoleic acid. J. Agric. Food Chem. 64:1355–60
Huang X, Kakuda Y, Cui W. 2001. Hydrocolloids in emulsions: particle size distribution and interfacial
activity. Food Hydrocoll. 15:533–42
Hunter RJ. 2001. Foundations of Colloid Science. Oxford, UK: Oxford Univ. Press
Jirku V, Cejkova A, Schreiberova O, Jezdik R, Masak J. 2015. Multicomponent biosurfactants: a “Green
Annu. Rev. Food Sci. Technol. 2017.8:205-236. Downloaded from www.annualreviews.org
based nanoemulsion formulation from selected cooking oils: evaluation for antimicrobial activity against
selected food associated microorganisms. J. Taiwan Inst. Chem. Eng. 43:172–80
Kaminogawa S, Shimizu M, Ametai A, Lee SW, Yamauchi K. 1987. Proteolysis in structural analysis of αs1 -
casein adsorbed onto oil surfaces of emulsions and improvement of the emulsifying properties of protein.
J. Am. Oil Chem. Soc. 64:1688–91
Karaca AC, Low NH, Nickerson MT. 2015. Potential use of plant proteins in the microencapsulation of
lipophilic materials in foods. Trends Food Sci. Technol. 42:5–12
Kargar M, Spyropoulos F, Norton IT. 2011. The effect of interfacial microstructure on the lipid oxidation
stability of oil-in-water emulsions. J. Colloid Interface Sci. 357:527–33
Karim A, Bhat R. 2009. Fish gelatin: properties, challenges, and prospects as an alternative to mammalian
gelatins. Food Hydrocoll. 23:563–76
Kayitmazer AB, Seeman D, Minsky BB, Dubin PL, Xu Y. 2013. Protein-polyelectrolyte interactions. Soft Mat-
ter 9:2553–83
Keerati-u-rai M, Corredig M. 2009. Heat-induced changes in oil-in-water emulsions stabilized with soy
protein isolate. Food Hydrocoll. 23:2141–48
Keerati-u-rai M, Corredig M. 2010. Heat-induced changes occurring in oil/water emulsions stabilized by soy
glycinin and β-conglycinin. J. Agric. Food Chem. 58:9171–80
Kim HJ, Decker EA, McClements DJ. 2002a. Impact of protein surface denaturation on droplet flocculation
in hexadecane oil-in-water emulsions stabilized by β-lactoglobulin. J. Agric. Food Chem. 50:7131–37
Kim HJ, Decker EA, McClements DJ. 2002b. Role of postadsorption conformation changes of β-lactoglobulin
on its ability to stabilize oil droplets against flocculation during heating at neutral pH. Langmuir 18:7577–
83
Kizilay E, Kayitmazer AB, Dubin PL. 2011. Complexation and coacervation of polyelectrolytes with oppositely
charged colloids. Adv. Colloid Interface Sci. 167:24–37
Klang V, Valenta C. 2011. Lecithin-based nanoemulsions. J. Drug Deliv. Sci. Technol. 21:55–76
Klinkesorn U. 2013. The role of chitosan in emulsion formation and stabilization. Food Rev. Int. 29:371–93
Komaiko J, Sastrosubroto A, McClements DJ. 2015. Formation of oil-in-water emulsions from natural emul-
sifiers using spontaneous emulsification: sunflower phospholipids. J. Agric. Food Chem. 63:10078–88
Komaiko J, Sastrosubroto A, McClements DJ. 2016. Encapsulation of ω-3 fatty acids in nanoemulsion-based
delivery systems fabricated from natural emulsifiers: sunflower phospholipids. Food Chem. 203:331–39
Kralova I, Sjoblom J. 2009. Surfactants used in food industry: a review. J. Dispers. Sci. Technol. 30:1363–83
Lam RSH, Nickerson MT. 2013. Food proteins: a review on their emulsifying properties using a structure-
function approach. Food Chem. 141:975–84
Lang S. 2002. Biological amphiphiles (microbial biosurfactants). Curr. Opin. Colloid Interface Sci. 7:12–20
Leroux J, Langendorff V, Schick G, Vaishnav V, Mazoyer J. 2003. Emulsion stabilizing properties of pectin.
Food Hydrocoll. 17:455–62
232 McClements · ·
Bai Chung
FO08CH11-McClements ARI 31 January 2017 9:55
Liang Y, Wong S-S, Pham SQ, Tan JJ. 2016. Effects of globular protein type and concentration on the
physical properties and flow behaviors of oil-in-water emulsions stabilized by micellar casein–globular
protein mixtures. Food Hydrocoll. 54:89–98
Liang YC, Gillies G, Patel H, Matia-Merino L, Ye AQ, Golding M. 2014. Physical stability, microstructure
and rheology of sodium-caseinate-stabilized emulsions as influenced by protein concentration and non-
adsorbing polysaccharides. Food Hydrocoll. 36:245–55
Lam RS, Nickerson MT. 2015. The effect of pH and temperature pre-treatments on the structure, surface
characteristics and emulsifying properties of α-lactalbumin. Food Chem. 173:163–70
Lin XJ, Wang Q, Li WL, Wright AJ. 2014. Emulsification of algal oil with soy lecithin improved DHA
bioaccessibility but did not change overall in vitro digestibility. Food Funct. 5:2913–21
Liu W, Ye A, Singh H. 2015. Progress in applications of liposomes in food systems. In Microencapsulation and
Microspheres for Food Applications, ed. LMC Sagis, pp. 151–72. Amsterdam: Elsevier
Lovaglio RB, dos Santos FJ, Jafelicci M, Contiero J. 2011. Rhamnolipid emulsifying activity and emulsion
Annu. Rev. Food Sci. Technol. 2017.8:205-236. Downloaded from www.annualreviews.org
Nielsen NS, Horn AF, Jacobsen C. 2013. Effect of emulsifier type, pH and iron on oxidative stability of 5%
fish oil-in-water emulsions. Eur. J. Lipid Sci. Technol. 115:874–89
Nishinari K, Fang Y, Guo S, Phillips GO. 2014. Soy proteins: a review on composition, aggregation and
emulsification. Food Hydrocoll. 39:301–18
Nitschke M, Costa S. 2007. Biosurfactants in food industry. Trends Food Sci. Technol. 18:252–59
Nitschke M, Costa S, Contiero J. 2010. Structure and applications of a rhamnolipid surfactant produced in
soybean oil waste. Appl. Biochem. Biotechnol. 160:2066–74
Niu F, Niu D, Zhang H, Chang C, Gu L, et al. 2016. Ovalbumin/gum arabic–stabilized emulsion: rheology,
emulsion characteristics, and Raman spectroscopic study. Food Hydrocoll. 52:607–14
Norde W. 2011. Colloids and Interfaces in Life Sciences and Bionanotechnology. Boca Raton, FL: CRC Press.
495 pp.
Ogawa S, Decker EA, McClements DJ. 2003a. Influence of environmental conditions on the stability of oil
in water emulsions containing droplets stabilized by lecithin-chitosan membranes. J. Agric. Food Chem.
Annu. Rev. Food Sci. Technol. 2017.8:205-236. Downloaded from www.annualreviews.org
51:5522–27
Ogawa S, Decker EA, McClements DJ. 2003b. Production and characterization of O/W emulsions containing
Access provided by University of Melbourne on 02/24/20. For personal use only.
234 McClements · ·
Bai Chung
FO08CH11-McClements ARI 31 January 2017 9:55
Ribeiro IA, Castro MF, Ribeiro MH. 2013. Sophorolipids: production, characterization and biologic activity.
In Applications of Microbial Engineering, ed. VK Gupta, MA Mazutti, M Maki, MG Tuohy, pp. 367–407.
Boca Raton, FL: CRC Press
Rosenberg E, Ron EZ. 1999. High- and low-molecular-mass microbial surfactants. Appl. Microbiol. Biotechnol.
52:154–62
Saeedi LH, Assadi MM, Heydarian SM, Jahangiri M. 2014. The production and evaluation of a nano-
biosurfactant. Petroleum Sci. Technol. 32:125–32
Sagalowicz L, Leser ME. 2010. Delivery systems for liquid food products. Curr. Opin. Colloid Interface Sci.
15:61–72
Salas C, Nypeloe T, Rodriguez-Abreu C, Carrillo C, Rojas OJ. 2014. Nanocellulose properties and applications
in colloids and interfaces. Curr. Opin. Colloid Interface Sci. 19:383–96
Salminen H, Aulbach S, Leuenberger BH, Tedeschi C, Weiss J. 2014. Influence of surfactant composition on
physical and oxidative stability of quillaja saponin–stabilized lipid particles with encapsulated omega-3
Annu. Rev. Food Sci. Technol. 2017.8:205-236. Downloaded from www.annualreviews.org
reduction, acetylation and esterification on the emulsification properties of citrus pectin. Food Biophys.
10:217–27
Schmidt US, Schmidt K, Kurz T, Endress HU, Schuchmann HP. 2015b. Pectins of different origin and their
performance in forming and stabilizing oil-in-water-emulsions. Food Hydrocoll. 46:59–66
Sidhu G, Oakenfull D. 1986. A mechanism for the hypocholesterolaemic activity of saponins. Br. J. Nutr.
55:643–49
Sifour M, Al-Jilawi MH, Aziz GM. 2007. Emulsification properties of biosurfactant produced from Pseudomonas
aeruginosa RB 28. Pak. J. Biol. Sci. 10:1331–35
Srinivasan M, Singh H, Munro P. 2002. Formation and stability of sodium caseinate emulsions: influence of
retorting (121 C for 15 min) before or after emulsification. Food Hydrocoll. 16:153–60
Stauffer SE. 1999. Emulsifiers. St Paul, MN: Eagan Press
Taherian AR, Britten M, Sabik H, Fustier P. 2011. Ability of whey protein isolate and/or fish gelatin to inhibit
physical separation and lipid oxidation in fish oil-in-water beverage emulsion. Food Hydrocoll. 25:868–78
Tcholakova S, Denkov ND, Lips A. 2008. Comparison of solid particles, globular proteins and surfactants as
emulsifiers. Phys. Chem. Chem. Phys. 10:1608–27
Tchuenbou-Magaia FL, Norton IT, Cox PW. 2009. Hydrophobins stabilised air-filled emulsions for the food
industry. Food Hydrocoll. 23:1877–85
Teo A, Goh KK, Wen J, Oey I, Ko S, et al. 2016. Physicochemical properties of whey protein, lactoferrin and
Tween 20 stabilised nanoemulsions: effect of temperature, pH and salt. Food Chem. 197:297–306
Tokle T, McClements DJ. 2011. Physicochemical properties of lactoferrin stabilized oil-in-water emulsions:
effects of pH, salt and heating. Food Hydrocoll. 25:976–82
Torabizadeh H, Shojaosadati SA, Tehrani HA. 1996. Preparation and characterisation of bioemulsifier from
Saccharomyces cerevisiae and its application in food products. LWT Food Sci. Technol. 29:734–37
Torrego-Solana N, Garcia-Celma MJ, Garreta A, Marques AM, Diaz P, Manresa A. 2014. Rhamnolipids
obtained from a PHA-negative mutant of Pseudomonas aeruginosa 47T2 delta AD: composition and emul-
sifying behavior. J. Am. Oil Chem. Soc. 91:503–11
Uluata S, McClements DJ, Decker EA. 2015. Physical stability, autoxidation, and photosensitized oxidation
of omega-3 oils in nanoemulsions prepared with natural and synthetic surfactants. J. Agric. Food Chem.
63:9333–40
Uzoigwe C, Burgess JG, Ennis CJ, Rahman PK. 2015. Bioemulsifiers are not biosurfactants and require
different screening approaches. Front. Microbiol. 6:245
Van Bogaert INA, Saerens K, De Muynck C, Develter D, Soetaert W, Vandamme EJ. 2007. Microbial
production and application of sophorolipids. Appl. Microbiol. Biotechnol. 76:23–34
Van Bogaert INA, Zhang J, Soetaert W. 2011. Microbial synthesis of sophorolipids. Process Biochem. 46:821–33
Varvaresou A, Iakovou K. 2015. Biosurfactants in cosmetics and biopharmaceuticals. Lett. Appl. Microbiol.
61:214–23
Velikov KP, Pelan E. 2008. Colloidal delivery systems for micronutrients and nutraceuticals. Soft Matter
4:1964–80
Waller GR, Yamasaki K. 1996a. Saponins Used in Food and Agriculture. New York: Plenum Press
Waller GR, Yamasaki K. 1996b. Saponins Used in Traditional and Modern Medicine. New York: Plenum Press
Waraho T, McClements DJ, Decker EA. 2011. Mechanisms of lipid oxidation in food dispersions. Trends Food
Sci. Technol. 22:3–13
Washington C. 1996. Stability of lipid emulsions for drug delivery. Adv. Drug Deliv. Rev. 20:131–45
Washington C, Chawla A, Christy N, Davis SS. 1989. The electrokinetic properties of phospholipid-stabilized
fat emulsions. Int. J. Pharm. 54:191–97
Wiacek AE, Adryanczyk E. 2015. Interfacial properties of phosphatidylcholine-based dispersed systems.
Ind. Eng. Chem. Res. 54:6489–96
Wierenga PA, Egmond MR, Voragen AGJ, de Jongh HH. 2006. The adsorption and unfolding kinetics
determines the folding state of proteins at the air-water interface and thereby the equation of state.
J. Colloid Interface Sci. 299:850–57
Wilde PJ. 2009. Emulsions and nanoemulsions using dairy ingredients. In Dairy-Derived Ingredients: Food
Nutraceutical Uses, ed. M Corredig, pp. 539–64. Cambridge, UK: Woodhead Publ.
Annu. Rev. Food Sci. Technol. 2017.8:205-236. Downloaded from www.annualreviews.org
Williams PA, Phillips GO. 2009. Gum arabic. In Handbook of Hydrocolloids, ed. PA Williams, GO Phillips,
Access provided by University of Melbourne on 02/24/20. For personal use only.
236 McClements · ·
Bai Chung
FO08-TOC ARI 4 February 2017 11:39
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