Recent Advances in The Utilization of Natural Emulsifiers To Form and Stabilize Emulsions

FO08CH10-McClements ARI 4 January 2017 12:11
Review in Advance first posted online

V I E W
E on January 11, 2017. (Changes may
R
still occur before final publication
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online and in print.)
C E
I N
A
D V A
Recent Advances in the

Utilization of Natural
Emulsifiers to Form and
Stabilize Emulsions
Annu. Rev. Food Sci. Technol. 2017.8. Downloaded from www.annualreviews.org
Access provided by Fudan University on 01/18/17. For personal use only.
David Julian McClements,1 Long Bai,1,2

and Cheryl Chung1
1
Department of Food Science, University of Massachusetts, Amherst, Massachusetts 01060;
email: mcclements@foodsci.umass.edu
2
College of Material Science and Engineering, Northeast Forestry University, Harbin 150040,
People’s Republic of China
Annu. Rev. Food Sci. Technol. 2017. 8:10.1–10.32 Keywords

The Annual Review of Food Science and Technology is proteins, polysaccharides, phospholipids, biosurfactants, Pickering
online at food.annualreviews.org
stabilization
This article’s doi:
10.1146/annurev-food-030216-030154 Abstract
Copyright c 2017 by Annual Reviews. Consumer concern about human and environmental health is encouraging
All rights reserved
food manufacturers to use more natural and sustainable food ingredients.
In particular, there is interest in replacing synthetic ingredients with natu-
ral ones, and in replacing animal-based ingredients with plant-based ones.
This article provides a review of the various types of natural emulsifiers with
potential application in the food industry, including phospholipids, biosur-
factants, proteins, polysaccharides, and natural colloidal particles. Increased
utilization of natural emulsifiers in food products may lead to a healthier and
more sustainable food supply. However, more research is needed to iden-
tify, isolate, and characterize new sources of commercially viable natural
emulsifiers suitable for food use.
10.1
Changes may still occur before final publication online and in print
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
required (McClements 2015a). Numerous types of stabilizers are available to improve emulsion
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.
Surface Pressure at Saturation

The surface pressure is the difference in interfacial tension at an oil-water interface in the presence
(γ) and absence (γ0 ) of emulsifier: = γ0 − γ. This value increases from zero to a constant
10.2 McClements · ·
Bai Chung
a Emulsion formation b Emulsion stabilization
Requirements: Requirements:
• Adsorb rapidly • Generate strong repulsive forces

• Lower interfacial tension • Form resistant interfacial layer

• Facilitate droplet breakup • Prevent droplet aggregation
Figure 1
Emulsifiers play two key roles in the production of commercial emulsion-based food products: They
(a) facilitate emulsion formation and (b) promote emulsion stability.
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
www.annualreviews.org • Recent Advances in the Utilization 10.3
Lecithin
Saponins
4 Gum arabic
Mean particle diameter, d32 (μm)

Whey protein
1
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).
Bai Chung
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
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.
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).
Emulsion formation. The hydrophile-lipophile balance (HLB) number of lecithins depends on

the head and tail group types. Many natural lecithins have HLB numbers around seven, which
means they can be dispersed in both oil and water phases. The effectiveness of lecithins at forming
emulsions may therefore depend on whether they are dispersed in the oil or water phase prior to
homogenization. At present, there is no clear understanding of which phase is the best, and thus
this factor has to be empirically established for a particular system. Lysolecithins tend to have
higher HLB numbers than lecithins and are therefore usually dispersed in the water phase prior
to homogenization.
The effectiveness of lecithins at forming oil-in-water emulsions is highly system dependent.
Some lecithins are very poor emulsifiers, whereas others work well. Emulsions containing large
oil droplets (e.g., 10 to 100 μm) have been formed from lecithin using high shear mixers (Guiotto
et al. 2013, Pan et al. 2004), whereas emulsions containing small droplets (<500 nm) have been
formed using high-pressure valve homogenizers, microfluidizers, or sonicators (Heo et al. 2016,
Klang & Valenta 2011, Lin et al. 2014, Ozturk et al. 2014, Washington 1996). Typically, the size
of the droplets formed during homogenization decreases with increasing emulsifier concentration,
homogenization pressure, and homogenization duration (Cabezas et al. 2012, Guiotto et al. 2013,
Komaiko et al. 2016, Mezdour et al. 2011, Washington 1996). However, the impact of emulsifier
concentration on droplet size and emulsion structure depends on lecithin type. For example,
certain types of sunflower lecithin form single phospholipid layers around fat droplets when used
at low levels but form multilayers at the droplet surfaces, and vesicles are in the aqueous phase
at high levels (Komaiko et al. 2016, Pan et al. 2004). These multilayers and vesicles influence
the physiochemical properties of emulsions by altering their texture, appearance, or stability.
Oil-in-water emulsions can also be formed from sunflower lecithins using low-energy methods
(spontaneous emulsification), but the fat droplets created are relatively large (>10 μm) (Komaiko
et al. 2015).
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
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
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
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., sugars groups) parts low levels via high-energy 1997, Ozturk
saponaria tree and hydrophobic (e.g., emulsification methods. et al. 2014)
triterpenoid rings) parts on Unstable under acidic
the same molecule conditions (pH < 3) and high
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 )
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
chloride)
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
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
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 )
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)
making up 60–65% of MW ≈ 45 kDa; pI ≈ 4.5; high ionic strengths, and at
the total protein Tm ≈ 80◦ C high temperatures (>Tm )

Lysozyme Egg white Globular protein Unstable at pH near pI, at (Zhang et al.
MW ≈ 14.3 kDa; pI ≈ 11.3; high ionic strengths, and at 2015d)
Tm ≈ 72◦ C high temperatures (>Tm )
Soy protein Soybeans Mixture of globular proteins Form fairly small droplets at (Bellesi et al. 2016,
(35–40% protein) with wide range of molecular low concentrations. Unstable Fernandez-Avila
weights at pH near pI, at high ionic et al. 2015,
pI ≈ 4.5; Tm ≈ 90◦ C strengths, and at high Keerati-u-rai &
temperatures (>Tm ) Corredig 2010)
Pea protein Peas Mixture of globular proteins Form small droplets at high (Benjamin et al.
(20–30% protein) with wide range of molecular concentrations. Unstable at 2014, Donsiı́
weights pH near pI and at et al. 2010)
pI ≈ 4.8; Tm ≈ 82◦ C temperatures (>Tm )
Lupin protein Lupin beans Globular proteins: consisting Form small droplets at (Benjamin et al.
(35–40% protein) mainly of globulin (70%) relatively low concentration. 2014, Raikos
followed by albumin (<20%) Emulsion stability affected by et al. 2014)
storage proteins. pH, unstable at pH near pI
Gelatin Animal sources (collagen) Fairly hydrophilic flexible Often not very surface active (Karim & Bhat
proteins with variable because of high hydrophilic 2009)
molecular weights character
depending on processing
conditions
pI ≈ 5 (Type B) or 8
(Type A); Tm ≈ 10–30◦ C
Polysaccharides
Gum arabic Derived from the Acacia Consisting of hydrophobic Form micron or submicron (Ozturk et al.
senegal tree protein part and hydrophilic droplets at high 2015a, Williams
polysaccharide parts on the surfactant-to-oil ratio via & Phillips 2009)
same molecule high-energy emulsification
MW ≈ 1,000 kDa; pKa ≈ 3.5 methods. Stable over a wide
range of pH, ionic strength,
and temperature
(Continued )
Bai Chung
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
hydrophobic protein groups high-energy emulsifier
methods. Stable over a wide

range of environmental
stresses (pH, ionic strength,
and temperature)
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
Relative mean particle diameter, d/dinitial

Q-Naturale® Q-Naturale®
30 Gum arabic Gum arabic
Whey protein Whey protein
102
ζ-potential (mV)
10
–10
101
–30
100
–50
–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.
Biosurfactants and Bioemulsifiers

A number of small surface-active molecules can be isolated from natural sources, e.g., glycolipids,
lipoproteins, and lipopeptides (De et al. 2015, Nitschke & Costa 2007, Varvaresou & Iakovou
Bai Chung
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, 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).
Bioemulsifiers are high-molecular-weight surface-active substances isolated from microbial
sources, which typically include proteins, polysaccharides, lipopolysaccharides, and lipoproteins
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).
Sophorolipids. Sophorolipids are glycolipids produced by some species of microorganisms, par-

ticularly yeasts (de Oliveira et al. 2015, Rosenberg & Ron 1999). They can be produced on an
industrial scale using microbial fermentation processes utilizing suitable yeast strains (such as
Candida batistae and Candida bombocola) and substrates (such as carbon and nitrogen sources) (de
Oliveira et al. 2015, De et al. 2015). These molecules consist of a hydrophilic sophorose group
(a disaccharide) attached to a hydrophobic hydrocarbon tail (a fatty acid chain) (de Oliveira et al.
2015). The nature of the sophorose head group and hydrocarbon tails depends on the microbial
strain, fermentation conditions, and substrates used, which leads to biosurfactants with differ-
ent physicochemical and functional properties (Lang 2002, Ribeiro et al. 2013). The sophorose
component can have different degrees of acetylation, and the fatty acid chain can have different
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
HO OH
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.
Mannoproteins. Mannoproteins are categorized as bioemulsifiers because of their higher molec-

ular weight (14–15.8 kDa) than biosurfactants. Mannoproteins are major structural components
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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
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
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).
Sophorolipids. Sophorolipids are predominately hydrophilic biosurfactants with a reported HLB

number of approximately 10 to 13 (Van Bogaert et al. 2007) and may therefore be suitable for
stabilizing oil-in-water emulsions. Sophorolipids reduce the surface tension at the air-water inter-
face from 73 mN/m to approximately 30 or 40 mN/m and have a critical micelle concentration of
approximately 40–100 mg/L (Van Bogaert et al. 2007). There have been few systematic studies of
the ability of sophorolipids to form stable oil-in-water emulsions. Sophorolipids form emulsions
containing large oil droplets when prepared by simple vortexing (Daverey & Pakshirajan 2010,
Morya et al. 2013) but form emulsions containing small oil droplets (d32 < 320 nm) when prepared
by microfluidization (Xue et al. 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 oil-
in-water emulsions that are stable over a range of pH values, ionic strengths, and temperatures (Oz-
turk et al. 2014, Yang et al. 2013, Yang & McClements 2013). In the absence of salt, saponin-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.
Rhamnolipids. The influence of pH on the stability of oil-in-water emulsions formed using a

rhamnolipid has been examined (Lovaglio et al. 2011). However, the emulsions were produced
using a simple shaking method, and thus the droplets were initially rather large. The emulsions
were relatively stable to coalescence from pH 5 to pH 9 but unstable at pH 3 to pH 5. This
effect may have been due to a loss of negative charge on the rhamnolipids with decreasing pH. A
more recent study reported that rhamnolipid-coated lipid droplets in nanoemulsions were stable
to aggregation from pH 5 to pH 9, from 0 to 100-mM NaCl, and from 20 to 90◦ C, but were
unstable at lower pH values and higher salt levels (Bai & McClements 2016). The stability of
these systems was related to the impact of pH and salt on the electrostatic repulsion between the
droplets.
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-
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,
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 lead to poor water solubility, whereas too few nonpolar groups lead 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
a Surface-active lipids b Surface-active biopolymers
Water – – –
–
–
Oil
Saponins Polysaccharides
– – – – – –
Phospholipids Flexible proteins
– – – – – –
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
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
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, Donsı́
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-,
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
Mean particle diameter, d32 (μm)

25 Lentil Lentil
20 +
Pea Pea
15 + +
ζ-potential (mV)
15
5 pI
10
–5 –
–
– 5 –
–15
–25 0
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
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
some food applications (Gomez-Guillen et al. 2011, Taherian et al. 2011).
The emulsifying properties of plant-based proteins isolated from a variety of sources have
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 non-polar groups on the same molecule, such as
gum arabic, beet pectin, and modified starch.
Molecular and physicochemical characteristics. The functional performance of a particular

polysaccharide depends on its molar mass, degree of branching, electrical charge, hydrophobicity,
and polarity. Many polysaccharides are not particularly good emulsifiers because they primarily
consist of polar monosaccharides. However, some polysaccharides have protein (glycoproteins)
or lipid (glycolipids) groups covalently bonded to them that provide some hydrophobicity. As a
result, these polysaccharides are amphiphilic molecules that can adsorb to oil-water interfaces and
stabilize emulsions.
The most widely used natural polysaccharide emulsifier in food and beverage applications is
gum arabic (Nie et al. 2013, Patel & Goyal 2015, Williams & Phillips 2009). Gum arabic is com-
mercially available as a powder or as granules that are dissolved in the aqueous phase prior to
homogenization. Gum arabic consists of a hydrophobic polypeptide backbone (that anchors it to
oil droplet surfaces) covalently attached to numerous hydrophilic anionic polysaccharide chains
(which provide steric and electrostatic stabilization). The emulsifying properties of gum arabic
can be improved using processing methods, such as controlled humidity and thermal processing
treatments (Xiang et al. 2015). Other types of polysaccharide-based emulsifiers are also commer-
cially available for utilization within foods and beverages, such as modified starch and modified
cellulose (Piorkowski & McClements 2014). However, both of these emulsifiers are not truly
natural because they are manufactured by chemically attaching nonpolar chains to the starch or
cellulose molecules. For this reason, these emulsifiers are not considered further.
There is considerable interest in the identification of new sources of amphiphilic polysac-
charides for use as natural food emulsifiers. Pectins isolated from various plants (such as apples,
oranges, okra, and sugar beet) can form and stabilize oil-in-water emulsions (Alba et al. 2013;
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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.
Emulsion formation. Amphiphilic polysaccharides are typically relatively large molecules that
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 d32
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).
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
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.
Natural Colloidal Particles

Numerous studies have shown that some natural colloidal particles can be used to form and stabilize
oil-in-water emulsions (Berton-Carabin & Schroen 2015, Dickinson 2012). These particles adsorb
to oil-water interfaces because their surfaces are wetted by both oil and water (Figure 8). If the
colloidal particles are wetted better by water than oil, then they protrude into the aqueous phase
and can stabilize oil-in-water emulsions. Various types of natural colloidal particles have been
identified as having potential to stabilize oil-in-water emulsions, such as chitin (Perrin et al. 2014,
Zhang et al. 2015c), cellulose (Salas et al. 2014), starch (Haaj et al. 2014), zein (de Folter et al.
2012), and cocoa (Gould et al. 2013) particles. Part of the motivation for developing these Pickering
emulsions is that they are often highly stable to coalescence because the colloidal particles stick
to the oil droplet surfaces so strongly. However, a major limitation is that only emulsions with
relatively large oil droplets (d > 2 μm) can be formed. Hence, research is ongoing to identify other
sources of natural colloidal particles that can be used to produce emulsions with small droplets
(Berton-Carabin & Schroën 2015).
Natural Emulsifier Combinations

Some natural emulsifiers are ineffective at forming and/or stabilizing oil-in-water emulsions when
used in isolation but are effective when used in combination with other natural substances. Dif-
ferent combination approaches can be adopted to improve emulsifier functionality.
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
Increasing oil wettability of particles

Oil phase
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.
Complexation/Conjugation. The effectiveness of natural emulsifiers can sometimes be im-

proved by forming physical or covalent complexes with other substances (Dickinson 2011). These
complexes can be created before or after homogenization. For example, a natural emulsifier can be
complexed with another component prior to homogenization, and then the emulsion is formed.
Alternatively, an emulsion can be formed using a natural emulsifier, and then the emulsifier is
complexed with another component after homogenization. For example, protein-carbohydrate
conjugates formed using the Maillard reaction can form small droplets that are stable over a
wide range of pHs, ionic strengths, and temperatures (Gumus et al. 2016, Wooster & Augustin
2006). The formation of protein-carbohydrate complexes through electrostatic attraction can also
improve the stability of emulsions to environmental stresses (Dickinson 2003).
Layer-by-layer deposition. The performance of emulsions stabilized by natural emulsifiers can

often be improved by creating multilayer coatings around them using electrostatic deposition
(Guzey & McClements 2006). An oil-in-water emulsion is first formed using an electrically
charged natural emulsifier (such as a biosurfactant, phospholipid, or protein). This emulsion is
then mixed with a solution containing oppositely charged polyelectrolytes (such as proteins or
polysaccharides). Under appropriate conditions, the polyelectrolyte molecules are deposited onto
the oil droplet surfaces because of electrostatic attraction. This process can be repeated numerous
times using polyelectrolytes with different charges to form nanolaminated coatings.
CONSIDERATIONS FOR DEVELOPING NEW NATURAL EMULSIFIERS

Numerous factors need to be considered when identifying a new source of natural emulsifiers for
utilization within the food industry.
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
and functionality vary widely from batch to batch depending on variations in their origin and
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).
Environmental and Safety Factors

A major advantage of natural emulsifiers is that they usually have better sustainability, biodegrad-
ability, and biocompatibility than synthetic surfactants (De et al. 2015, Kralova & Sjoblom 2009).
Consequently, they are more desirable to consumers wanting natural, or “green,” food products.
Natural emulsifiers are often less toxic than synthetic surfactants; however, they may still have
some toxicity and need to be carefully tested (De et al. 2015).
Regulatory and Marketing Issues

Many sectors of the food industry are trying to develop clean-label products containing more
label-friendly ingredients. The biological source of a natural emulsifier may impact a consumer‘s
perception of a product. Natural emulsifiers isolated from plants are often perceived as being more
label friendly than those obtained from animal or microbial sources. Natural emulsifiers should
also be legally acceptable for utilization within foods. Many natural emulsifiers are already widely
found in foods and are generally recognized as safe (GRAS), and thus can be utilized without any
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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.
CONCLUSIONS AND FUTURE DIRECTIONS

Consumers are demanding food and beverage products that are more natural and sustainable.
Consequently, the food industry is trying to replace many synthetic or animal-based emulsifiers
with natural plant-based alternatives. In this review, we have provided an overview of different
kinds of natural emulsifiers that can be used to form and stabilize oil-in-water emulsions, such
as phospholipids, biosurfactants, bioemulsifiers, proteins, polysaccharides, and colloidal particles.
These emulsifiers differ considerably in their ability to form small droplets during homogenization
that are stable to environmental stresses during storage, transport, and utilization. They also
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
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, Schroen 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
Cameron DR, Cooper DG, Neufeld R. 1988. The mannoprotein of Saccharomyces cerevisiae is an effective
bioemulsifier. Appl. Environ. Microbiol. 54:1420–25
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
Bai Chung
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
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
from yeast isolated from sugar palm wine. ScienceAsia 36:312–18
Donsı́ F, Senatore B, Huang Q Ferrari G. 2010. Development of novel pea protein-based nanoemulsions for
delivery of nutraceuticals. J. Agric. Food Chem. 58:10653–60
Elshafie AE, Joshi SJ, Al-Wahaibi YM, Al-Bemani AS, Al-Bahry SN, et al. 2015. Sophorolipids production by
Candida bombicola ATCC 22214 and its potential application in microbial enhanced oil recovery. Front.
Microbiol. 6:1324
Erickson MC. 2008. Chemistry and function of phospholipids. In Food Lipids, ed. CC Akoh, pp. 39–62.
Boca Raton, FL: CRC Press
Farzi M, Emam-Djomeh Z, Mohammadifar MA. 2013. A comparative study on the emulsifying properties of
various species of gum tragacanth. Int. J. Biol. Macromol. 57:76–82
Fathi M, Mozafari MR, Mohebbi M. 2012. Nanoencapsulation of food ingredients using lipid based delivery
systems. Trends Food Sci. Technol. 23:13–27
Fernandez-Avila C, Escriu R, Trujillo AJ. 2015. Ultra-high pressure homogenization enhances physicochem-
ical properties of soy protein isolate–stabilized emulsions. Food Res. Int. 75:357–66
Filotheou A, Ritzoulis C, Avgidou M, Kalogianni EP, Pavlou A, Panayiotou C. 2015. Novel emulsifiers from
olive processing solid waste. Food Hydrocoll. 48:274–81
Frede K, Henze A, Khalil M, Baldermann S, Schweigert FJ, Rawel H. 2014. Stability and cellular uptake of
lutein-loaded emulsions. J. Funct. Foods 8:118–27
Funami T, Nakauma M, Ishihara S, Tanaka R, Inoue T, Phillips GO. 2011. Structural modifications of sugar
beet pectin and the relationship of structure to functionality. Food Hydrocoll. 25:221–29
Garcia-Moreno PJ, Horn AF, Jacobsen C. 2014. Influence of casein-phospholipid combinations as emulsifier
on the physical and oxidative stability of fish oil-in-water emulsions. J. Agric. Food Chem. 62:1142–52
Gharsallaoui A, Saurel R, Chambin O, Cases E, Voilley A, Cayot P. 2010. Utilisation of pectin coating to
enhance spray-dry stability of pea protein–stabilised oil-in-water emulsions. Food Chem. 122:447–54
Gomez-Guillen MC, Gimenez B, Lopez-Caballero ME, Montero MP. 2011. Functional and bioactive prop-
erties of collagen and gelatin from alternative sources: a review. Food Hydrocoll. 25:1813–27
Gould J, Vieira J, Wolf B. 2013. Cocoa particles for food emulsion stabilisation. Food Funct. 4:1369–75
Guiotto EN, Cabezas DM, Diehl BWK, Tomas MC. 2013. Characterization and emulsifying properties of
different sunflower phosphatidylcholine enriched fractions. Eur. J. Lipid Sci. Technol. 115:865–73
Gumus CE, Davidov-Pardo G, McClements DJ. 2016. Lutein-enriched emulsion-based delivery systems:
impact of Maillard conjugation on physicochemical stability and gastrointestinal fate. Food Hydrocoll.
60:38–49
Gutierrez JM, Gonzalez C, Maestro A, Sole I, Pey CM, Nolla J. 2008. Nano-emulsions: new applications and
optimization of their preparation. Curr. Opin. Colloid Interface Sci. 13:245–51
Guzey D, McClements DJ. 2006. Formation, stability and properties of multilayer emulsions for application
in the food industry. Adv. Colloid Interface Sci. 128:227–48
Haaj SB, Magnin A, Boufi S. 2014. Starch nanoparticles produced via ultrasonication as a sustainable stabilizer
in Pickering emulsion polymerization. RSC Adv. 4:42638–46
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
Toolbox” extension. Biotechnol. Adv. 33:1272–76
Joe MM, Bradeeba K, Parthasarathi R, Sivakumaar PK, Chauhan PS, et al. 2012. Development of surfactin
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
Bai Chung
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
stability: pH rules. Colloids Surf. B 85:301–05
Lumsdon SO, Green J, Stieglitz B. 2005. Adsorption of hydrophobin proteins at hydrophobic and hydrophilic
interfaces. Colloids Surf. B 44:172–78

Luo Y, Wang Q. 2014. Zein-based micro- and nano-particles for drug and nutrient delivery: a review. J. Appl.
Polym. Sci. 131:40696
Maher PG, Fenelon MA, Zhou Y, Haque K, Roos YH. 2011. Optimization of β-casein stabilized nanoemul-
sions using experimental mixture design. J. Food Sci. 76:C1108–17
Mao YY, McClements DJ. 2011. Modulation of bulk physicochemical properties of emulsions by hetero-
aggregation of oppositely charged protein-coated lipid droplets. Food Hydrocoll. 25:1201–9
McClements DJ. 2012. Advances in fabrication of emulsions with enhanced functionality using structural
design principles. Curr. Opin. Colloid Interface Sci. 17:235–45
McClements DJ. 2010. Emulsion design to improve the delivery of functional lipophilic components. Annu.
Rev. Food Sci. Technol. 1:241–69
McClements DJ. 2015a. Food Emulsions: Principles, Practices, and Techniques. Boca Raton, FL: CRC Press
McClements DJ. 2004. Protein-stabilized emulsions. Curr. Opin. Colloid Interface Sci. 9:305–13
McClements DJ. 2015b. Reduced-fat foods: the complex science of developing diet-based strategies for tackling
overweight and obesity. Adv. Nutr. 6:338S–52
McClements DJ, Gumus CE. 2016. Natural emulsifiers—biosurfactants, phospholipids, biopolymers, and
colloidal particles: molecular and physicochemical basis of functional performance. Adv. Colloid Interface
Sci. 234:3–26
McClements DJ, Monahan FJ, Kinsella JE. 1993. Disulfide bond formation affects stability of whey-protein
isolate emulsions. J. Food Sci. 58:1036–39
Medina-Torres L, Calderas F, Gallegos-Infante JA, González-Laredo RF, Rocha-Guzmán N. 2009. Stability
of alcoholic emulsions containing different caseinates as a function of temperature and storage time.
Colloids Surf. A 352:38–46
Mezdour S, Desplanques S, Relkin P. 2011. Effects of residual phospholipids on surface properties of a soft-
refined sunflower oil: application to stabilization of sauce-types’ emulsions. Food Hydrocoll. 25:613–19
Mitra S, Dungan SR. 1997. Micellar properties of quillaja saponin. 1. Effects of temperature, salt, and pH on
solution properties. J. Agric. Food Chem. 45:1587–95
Molina E, Papadopoulou A, Ledward D. 2001. Emulsifying properties of high pressure treated soy protein
isolate and 7S and 11S globulins. Food Hydrocoll. 15:263–69
Monahan FJ, McClements DJ, Kinsella JE. 1993. Polymerization of whey proteins in whey protein–stabilized
emulsions. J. Agric. Food Chem. 41:1826–29
Morya VK, Park JH, Kim TJ, Jeon S, Kim EK. 2013. Production and characterization of low molecular weight
sophorolipid under fed-batch culture. Bioresour. Technol. 143:282–88
Muller MM, Kugler JH, Henkel M, Gerlitzki M, Hormann B, et al. 2012. Rhamnolipids: next generation
surfactants? J. Biotechnol. 162:366–80
Nie SP, Wang C, Cui SW, Wang Q, Xie MY, Phillips GO. 2013. A further amendment to the classical core
structure of gum arabic (Acacia senegal ). Food Hydrocoll. 31:42–48
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.
51:5522–27
Ogawa S, Decker EA, McClements DJ. 2003b. Production and characterization of O/W emulsions containing
cationic droplets stabilized by lecithin-chitosan membranes. J. Agric. Food Chem. 51:2806–12

Ogawa S, Decker EA, McClements DJ. 2004. Production and characterization of O/W emulsions containing
droplets stabilized by lecithin-chitosan-pectin mutilayered membranes. J. Agric. Food Chem. 52:3595–600
Osano JP, Hosseini-Parvar SH, Matia-Merino L, Golding M. 2014. Emulsifying properties of a novel polysac-
charide extracted from basil seed (Ocimum bacilicum L.): effect of polysaccharide and protein content. Food
Ozturk B, Argin S, Ozilgen M, McClements DJ. 2014. Formation and stabilization of nanoemulsion-based
vitamin E delivery systems using natural surfactants: quillaja saponin and lecithin. J. Food Eng. 142:57–63
Ozturk B, Argin S, Ozilgen M, McClements DJ. 2015a. Formation and stabilization of nanoemulsion-based
vitamin E delivery systems using natural biopolymers: whey protein isolate and gum arabic. Food Chem.
188:256–63
Ozturk B, Argin S, Ozilgen M, McClements DJ. 2015b. Nanoemulsion delivery systems for oil-soluble
vitamins: influence of carrier oil type on lipid digestion and vitamin D-3 bioaccessibility. Food Chem.
187:499–506
Pan LG, Tomas MC, Anon MC. 2004. Oil-in-water emulsions formulated with sunflower lecithins: vesicle
formation and stability. J. Am. Oil Chem. Soc. 81:241–44
Pan Y, Tikekar RV, Nitin N. 2013. Effect of antioxidant properties of lecithin emulsifier on oxidative stability
of encapsulated bioactive compounds. Int. J. Pharm. 450:129–37
Park K-Y, Kim D-Y, Shin W-S. 2015. Roles of chondroitin sulfate in oil-in-water emulsions formulated using
bovine serum albumin. Food Sci. Biotechnol. 24:1583–89
Patel S, Goyal A. 2015. Applications of natural polymer gum arabic: a review. Int. J. Food Prop. 18:986–98
Perfumo A, Smyth T, Marchant R, Banat I. 2010. Production and roles of biosurfactants and bioemulsifiers
in accessing hydrophobic substrates. In Handbook of Hydrocarbon and Lipid Microbiology, ed. KM Timmis,
TJ McGenity, JR van der Meer, V de Lorenzo, pp. 1501–12. Berlin: Springer-Verlag
Perrin E, Bizot H, Cathala B, Capron I. 2014. Chitin nanocrystals for Pickering high internal phase emulsions.
Biomacromolecules 15:3766–71
Pichot R, Watson RL, Norton IT. 2013. Phospholipids at the interface: current trends and challenges. Int. J.
Mol. Sci. 14:11767–94
Piorkowski DT, McClements DJ. 2014. Beverage emulsions: recent developments in formulation, production,
and applications. Food Hydrocoll. 42:5–41
Pugnaloni LA, Dickinson E, Ettelaie R, Mackie AR, Wilde PJ. 2004. Competitive adsorption of proteins and
low-molecular-weight surfactants: computer simulation and microscopic imaging. Adv. Colloid Interface
Sci. 107:27–49
Qian C, Decker EA, Xiao H, McClements DJ. 2011. Comparison of biopolymer emulsifier performance in
formation and stabilization of orange oil-in-water emulsions. J. Am. Oil Chem. Soc. 88:47–55
Raikos V, Neacsu M, Russell W, Duthie G. 2014. Comparative study of the functional properties of lupin,
green pea, fava bean, hemp, and buckwheat flours as affected by pH. Food Sci. Nutr. 2:802–10
Bai Chung
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
fish oil. Colloids Surf. B 122:46–55
Schmidt US, Koch L, Rentschler C, Kurz T, Endress HU, Schuchmann HP. 2015a. Effect of molecular weight
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.
Williams PA, Phillips GO. 2009. Gum arabic. In Handbook of Hydrocolloids, ed. PA Williams, GO Phillips,
pp. 252–73. Cambridge, UK: Woodhead Publ.

Wong BT, Zhai J, Hoffmann SV, Aguilar M-I, Augustin M, et al. 2012. Conformational changes to deamidated
wheat gliadins and β-casein upon adsorption to oil-water emulsion interfaces. Food Hydrocoll. 27:91–101
Wooster TJ, Augustin MA. 2006. β-lactoglobulin–dextran Maillard conjugates: their effect on interfacial
thickness and emulsion stability. J. Colloid Interface Sci. 303:564–72
Wosten HAB, Scholtmeijer K. 2015. Applications of hydrophobins: current state and perspectives. Appl.
Microbiol. Biotechnol. 99:1587–97
Wu Y, Eskin NAM, Cui W, Pokharel B. 2015. Emulsifying properties of water soluble yellow mustard
mucilage: a comparative study with gum arabic and citrus pectin. Food Hydrocoll. 47:191–96
Xiang SP, Yao XL, Zhang WQ, Zhang K, Fang YP, et al. 2015. Gum arabic–stabilized conjugated linoleic acid
emulsions: emulsion properties in relation to interfacial adsorption behaviors. Food Hydrocoll. 48:110–16
Xue CL, Solaiman DKY, Ashby RD, Zerkowski J, Lee JH, et al. 2013. Study of structured lipid-based oil-in-
water emulsion prepared with sophorolipid and its oxidative stability. J. Am. Oil Chem. Soc. 90:123–32
Xue J, Zhong QX. 2014. Thyme oil nanoemulsions coemulsified by sodium caseinate and lecithin. J. Agric.
Food Chem. 62:9900–7
Yadav MP, Johnston DB, Hicks KB. 2009. Corn fiber gum: new structure/function relationships for this
potential beverage flavor stabilizer. Food Hydrocoll. 23:1488–93
Yadav MP, Parris N, Johnston DB, Hicks KB. 2008. Fractionation, characterization, and study of the emul-
sifying properties of corn fiber gum. J. Agric. Food Chem. 56:4181–87
Yang Y, Leser ME, Sher AA, McClements DJ. 2013. Formation and stability of emulsions using a natural
small molecule surfactant: quillaja saponin (Q-Naturale R
). Food Hydrocoll. 30:589–96
Yang Y, McClements DJ. 2013. Encapsulation of vitamin E in edible emulsions fabricated using a natural
surfactant. Food Hydrocoll. 30:712–20
Zeeb B, Fischer L, Weiss J. 2011. Cross-linking of interfacial layers affects the salt and temperature stability of
multilayered emulsions consisting of fish gelatin and sugar beet pectin. J. Agric. Food Chem. 59:10546–55
Zhang J, Bing L, Reineccius GA. 2016. Comparison of modified starch and quillaja saponins in the formation
and stabilization of flavor nanoemulsions. Food Chem. 192:53–59
Zhang J, Bing L, Reineccius GA. 2015a. Formation, optical property and stability of orange oil nanoemulsions
stabilized by quallija saponins. LWT Food Sci. Technol. 64:1063–70
Zhang J, Peppard TL, Reineccius GA. 2015b. Preparation and characterization of nanoemulsions stabilized
by food biopolymers using microfluidization. Flavour Fragr. J. 30:288–94
Zhang Y, Chen Z, Bian W, Feng L, Wu Z, et al. 2015c. Stabilizing oil-in-water emulsions with regenerated
chitin nanofibers. Food Chem. 183:115–21
Zhang C, Zhu Y, Zhang R, Xie Y, Wang K, Liu X. 2015d. Pickering emulsions stabilized by composite
nanoparticles prepared from lysozyme and dopamine modified poly (γ-glutamic acid): effects of pH value
on the stability of the emulsion and the activity of lysozyme. RSC Adv. 5:90651–58
Zou L, Akoh CC. 2013. Characterisation and optimisation of physical and oxidative stability of structured lipid-
based infant formula emulsion: effects of emulsifiers and biopolymer thickeners. Food Chem. 141:2486–94
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FO08CH10-McClements ARI 4 January 2017 12:11

Review in Advance first posted online

still occur before final publication

Recent Advances in the

David Julian McClements,1 Long Bai,1,2

Annu. Rev. Food Sci. Technol. 2017. 8:10.1–10.32 Keywords

Surface Pressure at Saturation

a Emulsion formation b Emulsion stabilization

• Adsorb rapidly • Generate strong repulsive forces

• Lower interfacial tension • Form resistant interfacial layer

www.annualreviews.org • Recent Advances in the Utilization 10.3

Mean particle diameter, d32 (μm)

Emulsion formation. The hydrophile-lipophile balance (HLB) number of lecithins depends on

www.annualreviews.org • Recent Advances in the Utilization 10.5

(one fatty acid tail group) on Unstable under acidic

www.annualreviews.org • Recent Advances in the Utilization 10.7

the total protein Tm ≈ 80◦ C high temperatures (>Tm )

methods. Stable over a wide

www.annualreviews.org • Recent Advances in the Utilization 10.9

Relative mean particle diameter, d/dinitial

Biosurfactants and Bioemulsifiers

Sophorolipids. Sophorolipids are glycolipids produced by some species of microorganisms, par-

www.annualreviews.org • Recent Advances in the Utilization 10.11

Mannoproteins. Mannoproteins are categorized as bioemulsifiers because of their higher molec-

Sophorolipids. Sophorolipids are predominately hydrophilic biosurfactants with a reported HLB

www.annualreviews.org • Recent Advances in the Utilization 10.13

Rhamnolipids. The influence of pH on the stability of oil-in-water emulsions formed using a

plication in a variety of emulsion-based food products (Cox & Kim 2013).

www.annualreviews.org • Recent Advances in the Utilization 10.15

a Surface-active lipids b Surface-active biopolymers

Phospholipids Flexible proteins

www.annualreviews.org • Recent Advances in the Utilization 10.17

Mean particle diameter, d32 (μm)

www.annualreviews.org • Recent Advances in the Utilization 10.19

Molecular and physicochemical characteristics. The functional performance of a particular

www.annualreviews.org • Recent Advances in the Utilization 10.21

Natural Colloidal Particles

Natural Emulsifier Combinations

Increasing oil wettability of particles

Complexation/Conjugation. The effectiveness of natural emulsifiers can sometimes be im-

Layer-by-layer deposition. The performance of emulsions stabilized by natural emulsifiers can

www.annualreviews.org • Recent Advances in the Utilization 10.23

CONSIDERATIONS FOR DEVELOPING NEW NATURAL EMULSIFIERS

Environmental and Safety Factors

Regulatory and Marketing Issues

CONCLUSIONS AND FUTURE DIRECTIONS

www.annualreviews.org • Recent Advances in the Utilization 10.25

of emulsion formulation. J. Agric. Food Chem. 59:13203–11

www.annualreviews.org • Recent Advances in the Utilization 10.27

selected food associated microorganisms. J. Taiwan Inst. Chem. Eng. 43:172–80

interfaces. Colloids Surf. B 44:172–78

www.annualreviews.org • Recent Advances in the Utilization 10.29

cationic droplets stabilized by lecithin-chitosan membranes. J. Agric. Food Chem. 51:2806–12

www.annualreviews.org • Recent Advances in the Utilization 10.31

pp. 252–73. Cambridge, UK: Woodhead Publ.

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