ELS EVI E R Current Opinion in Colloid & Interface Science 5 (2000) 176-181

www.elsevier.nl/locate/cocis

Interfaces: their role in foam and emulsion behaviour

P.J. Wilde"
Institute of Food Research, Norwich Research Park, Norwich NR4 7UA, UK

Abstract

In this paper, recent progress in our knowledge of how the interface influences the formation and stability of emulsions has
been reviewed. Attention was focused on the effect of molecular structure, interfacial rheology, competitive adsorption and
interfacial structure and composition.0 2000 Elsevier Science Ltd. All rights reserved.

Keywords: Interface; Protein; Surfactant; Competitive adsorption

1. Introduction and usually form a compact adsorbed layer with a

With the exception of microemulsions, liquid foams
and emulsions are in general, thermodynamically un-
stable. The immiscible dispersed phase will only re-
main as a fine dispersion for a finite period, as the
dispersed droplets or bubbles will eventually coalesce
and separate out into the component phases. The
period of stability strongly depends on the character-
istics of the interface separating the dispersed and
continuous phases. The interface is composed of sur-
face-active molecules, which can adsorb from the
dispersed or continuous phase. These molecules need
to be amphiphilic, and thus are attracted to the inter-
facial region so that their component hydrophilic and
hydrophobic moieties may associate with the respec-
tive polar and non-polar phases. There are two classes
of surface-active molecules, which can stabilise foams
and emulsions:
1. Surfactants - these include detergents, emulsi-
fiers and lipids. They may be water or oil soluble,
* Tel.: + 44-1603-255258; fax: + 44-1603-507723.
E-mail address: peter.wilde@bbsrc.ac.uk (P.J. Wilde).
low interfacial tension.
2. Polymers - amphiphilic macromolecules, the
most commonly used are proteins. They typically
form a visco-elastic, irreversibly adsorbed layer.
The creation of foams and emulsions essentially
requires the formation of fine bubbles or droplets.
Apart from the energy input and the physical proper-
ties of the component phases (e.g. viscosity), the main
factor controlling droplet size is the interfacial ten-
sion. Droplets become more deformable as the inter-
facial tension is lowered, making them easier to dis-
perse. The ability to create foams and emulsions has
been correlated with the rate of change of the interfa-
cial tension [l-31. The important timescales for foam
and emulsion formation can be sub-millisecond;
therefore, the ability of a surfactant or polymer to
adsorb rapidly is critical for foam and emulsion for-
mation.
The stabilisation of foams and emulsions against
coalescence require different surface properties.
Long-range repulsive forces can be in the form of
electrostatic or steric repulsion, which prevent the
close approach of dispersed phase particles. However,
in concentrated foams and emulsions, the long-range

1359-0294/00/$ - see front matter 0 2000 Elsevier Science Ltd. All rights reserved.
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 P.J. Wilde /Current Opinion in Colloid & Interface Science 5 (2000) 176-181
repulsion is overcome, and other stability mechanisms
become dominant. These mechanisms depend on the
class of molecule used to stabilise the adsorbed layer.
Surfactants stabilise foams and emulsions most effec-
tively if they form a fluid adsorbed layer. This allows
them to migrate to regions with a reduced surfactant
concentration, due to perturbation during creation,
mixing or transport processes. This is known as the
Marangoni mechanism. In contrast, polymers are most
effective when they form a solid visco-elastic adsorbed
layer. This is most commonly observed in proteins,
which adsorb, partially unfold and form strong inter-
actions. This results in a visco-elastic adsorbed layer,
the strength of which has been correlated with foam
and emulsion stability [4,5].
The unfolding of proteins at interfaces is influenced
by the structure in solution, such that flexible proteins
will unfold quickly and lower the interfacial tension
rapidly [5], whereas globular proteins, which have
more intramolecular bonds stabilising their structure,
unfold more slowly. However, they tend to form
stronger intermolecular interactions and stabilise
against coalescence very effectively [51. Changing the
solution structure by various means has been used as
a tool for improving protein functionality, probably by
inducing a change in adsorbed conformation.
A problem that occurs particularly in food foams
and emulsions, is that there is often a mixture of
polymers and surfactants competing for the interface.
In concentration regimes where a mixed polymer-
surfactant interface exists, a reduction in stability is
often observed. The underlying mechanism is thought
to be a competition between the two stability mecha-
nisms. The surfactants weaken the visco-elasticity of
the adsorbed protein layer [4,6-81, and the polymers
retard the fluidity of the surfactants. The result is a
foam or emulsion that is less stable than those formed
by the individual surfactants or polymers [9,10].
It is, therefore, not surprising that current progress
in this field has tended to concentrate on: (i) adsorbed
protein structure; (ii) the rheology; and (iii) the com-
position of interfaces. Therefore, I have reviewed the
current literature in this field in these specific areas.
2. Adsorbed protein structure
Secondary and tertiary structures of proteins in
solution can be easily determined using a range of
spectrometric techniques. The structure of adsorbed
proteins is more difficult due to various technical
complications. The signal intensity from a single in-
terface is usually small and the resultant signal to
noise ratio can make interpretation difficult. Mea-
surements of proteins adsorbed onto particles or
droplets creates light scattering problems. Vermeer
117
and Norde [ l l ] used an array of quartz plates to
increase the number of interfaces that could be inter-
rogated by circular dichroism. They showed that the
adsorbed immunoglobulin possessed a different spec-
trum depending on the nature of the surface. Moulin
et al. used a microfabricated cantilever to measure
the surface stress induced by proteins adsorbed onto
a gold substrate [12]. They could apparently follow
long-term unfolding and interaction processes, which
were found to be very different between immuno-
globulin and BSA, although no firm conclusions about
the source of these differences could be drawn.
The limitation of these techniques in foams and
emulsions was the correlation of behaviour at a solid
surface with that at a fluid one. If this could be done,
then it would be possible to explain the effects seen
by Murray and Liang [13]. They found that spray-dry-
ing protein solutions had a detrimental effect on foam
stability. This was supported by changes in their ad-
sorption behaviour suggesting a conformational
change induced by the drying process. The presence
of the sugar trehalose during drying seemed to have a
positive effect on foaming properties, especially for
P-lactoglobulin. The corresponding adsorption be-
haviour suggested that the trehalose protected the
proteins against denaturation. This has also been con-
firmed by Clarkson et al. where the presence of
trehalose was seen to protect against surface denatu-
ration induced by foaming [141, although they found
that this was a minor effect compared to the effects of
ionic strength and pH.
Small differences in protein structure can infer
major changes in functionality. The genetic variants
A, B and C of P-lactoglobulin differ by only two
amino acid residues, yet this was found to cause
significant changes in adsorption behaviour [ 151 and
emulsification properties [16]. The substitution of an
aspartic acid residue in variant A to a glycine in B at
residue 64 appears to increase the rate of adsorption,
and the development of an elastic interface of variant
B [151. Although variant B had poorer emulsification
properties, its long-term stability to coalescence was
higher [16].
3. Interfacial rheology
The surface rheology of adsorbed protein layers has
long been known to be important for the stabilisation
of foams and emulsions [4,17]. The visco-elastic
properties of the surface have often been correlated
with functionality [2-4,181. A recent review by Dickin-
son [19'1 brought together certain aspects of the
structure and surface rheology of proteins, and the
correlation with the formation and stability of foams
and emulsions. A fascinating article by Izmailova et
118 P.J. Wilde /Current Opinion in Colloid & Inte8ace Science 5 (2000)176-181
al. [20’] reviewed the contribution made by Rehbin-
der to this area and offered new results showing how
the coalescence stability of protein foams and emul-
sions can be directly related to the mechanical
properties of the adsorbed protein layer. Rehbinder
put forward the concept that the elasticity of protein
interfaces was responsible for their stabilising ability.
This concept was developed further with some new
results confirming the idea that it is not simply the
value of the elastic modulus that is important for
stability, but the stress at which the elasticity breaks
down. However care must also be taken, as some
proteins such as p-casein are excellent at stabilising
emulsions by steric repulsion, but have very poor
surface rheological properties [21].
The surface visco-elastic properties of proteins can
also be important for formation of and drainage from
foams. Prins [22’] showed, by using the overflowing
cylinder, that proteins can slow the flow of liquid
close to the surface. This can retard liquid drainage
from foams, and is thought to contribute to the slower
drainage rates observed in protein-stabilised foams
compared to those stabilised by surfactants. In addi-
tion, Prins also postulated that this ‘stagnant surface
behaviour’ enabled the bubbles and droplets to be
more easily dispersed when the surface tension was
taken into account. In the absence of protein, the
droplet break-up was strongly dependent on the rela-
tive viscosities of the continuous and dispersed phases.
In contrast, in the presence of protein, the droplets
were dispersed more easily and independently of liq-
uid viscosity. This clearly demonstrated the contribu-
tion made by the surface rheology of proteins to the
functionality of foams and emulsions.
The presence of surfactants will reduce the surface
visco-elasticity of adsorbed protein layers [4,6,7] often
resulting in a drop in coalescence stability [4,9,10,23].
Chen and Dickinson showed that by displacing pro-
teins from emulsion droplets, the visco-elasticity of
emulsion gels could be significantly reduced [24]. The
interaction between the emulsion droplets and the gel
matrix was thought to be influenced by the amount of
adsorbed protein. Protein adsorption and the devel-
opment of the visco-elastic surface can be significantly
affected by protein conformation. Roth et al. [25]
found that ageing and heat treating proteins at the
interface could result in higher surface viscosities,
depending on the temperature, and the length of heat
treatment. Certainly the interfaces heated to the
higher temperatures studied formed a more viscous
interface. Some of the more visco-elastic interfaces
were also more resistant to the effects of added
surfactant, although there was no clear correlation for
all the treatments studied. Petkov et al. demonstrated
a new method of simultaneously measuring the sur-
face dilational and shear parameters in protein films
[26]. Again, this technique demonstrates how sensitive
surface rheology is to the disruptive effects which
surfactants have on protein adsorbed layers. One way
to restore stability to a surfactant destabilised foam is
to restore the surface visco-elasticity. Propylene glycol
alginate (PGA) has been used to improve beer foam
stability. A detailed study of this improvement showed
that PGA restored the surface elasticity of a mixed
protein-surfactant interface [27]. This was thought to
be due to an electrostatic ‘crosslinking’ mechanism,
which partially restored the protein-protein interac-
tions that had been disrupted by the presence of
surfactant. The interfacial rheology of wheat proteins
is of importance to the baking industry. Yet a recent
review of the area [28] shows that there is distinct gap
in our knowledge on effect of their surface properties
on baking quality. It is likely, therefore, that the
surface properties of wheat proteins will receive much
attention in the near future.
It is not only the surface rheology of proteins that
is important to functionality. Recent studies on the
surface rheology of surfactants have also shown a
correlation with foam formation and stability. Kanicky
et al. [291 showed that sodium laurate solutions showed
maximal surface viscosity at pH values close to their
pK,. This corresponded with maximal foam forma-
tion, and foam stability. They showed that the interfa-
cial packing was highest at the pK,, as expected, as
the electrostatic repulsion between the molecules was
minimal. This also corresponded with improved emul-
sification and reduced water evaporation. Changing
the chain length of the sodium laurate changed the
pK, such that the foaming properties were more
dependent on the pH than the molecular structure of
the surfactant. Fruhner et al. studied a range of
different surfactants [30’]. By using the oscillating
bubble technique at high frequencies (up to 500 Hz),
they were able to obtain surface dilational visco-elas-
tic data for soluble surfactants. They found that the
surface needed to develop a significant viscous com-
ponent before the solutions were able to create a
stable foam. At very low concentrations, below that
which would support a stable foam, purely elastic
behaviour was observed. At high concentrations, the
surfactants which were able to support foams such as
SDS, CTAB and Triton-X 100, developed a viscous
component. Surfactants which did not form stable
foams, such as nonanol and dodecanol, remained
purely elastic. The differences are thought to be due
to the improved hydration of the headgroups belong-
ing to the foam active group of surfactants.
4. Surface composition and structure
Competitive destabilisation of proteins by surfac-
 P.J. Wilde /Current Opinion in Colloid & Interface Science 5 (2000) 176-181
tants has been an area of intense interest in food
colloids for many years [4,6,9,10,231. Although it is
known that surfactants reduce the surface visco-elas-
ticity of protein films, as discussed in Section 3, until
recently, however, the mechanisms underlying this
effect remained elusive. Our understanding of the
competitive adsorption mechanism has been signifi-
cantly advanced recently by the ability to visualise the
structure of mixed protein-surfactant interfaces.
Atomic force microscopy (AFM) is a powerful
method for imaging surface detail on flat substrates at
molecular resolution. It has been used to study pro-
tein adsorption onto both solid [31] and liquid inter-
faces [32]. Recent work by Morris et al. [33",34']
have been able to image mixed protein-surfactant
interfaces. In contrast to the assumption that mixed
interfaces contain a homogenous distribution of pro-
tein and surfactant, these studies clearly show a
demixing phenomenon, an example of which is shown
in Fig. 1. The power of the technique is that it can
impart interfacial thickness information with ex-
tremely high spatial resolution. This has led to the
proposed 'orogenic' model of protein displacement.
The observations showed that the surfactant domains
exerted a lateral surface pressure and compressed
protein regions. As more surfactant was adsorbed, the
surface pressure increased until the protein regions
collapsed and were eventually displaced. These stud-
ies have helped explain: (i) why the stability of protein
foams and emulsions is often affected at very low
concentrations of surfactant, before any protein is
displaced [10,231; (ii) observed increases in the thick-
ness or concentration of adsorbed protein layers
observed in mixed protein-surfactant interfaces
[19,35']; and (iii) why proteins with a higher visco-
elastic modulus are more difficult to displace [lo]. The
Fig. 1. AFM image of a Langmuir-Blodgett film of a mixed p-
lactoglobulin-Tween 20 film at the air-water interface. The light
regions denote the surfactant domains, and the dark regions repre-
sent the thicker protein regions. Image size is 2 x 2 pm.
179
Fig. 2. Brownian dynamic simulation of the competitive displace-
ment of protein-like (dark) particles, by surfactant-like displacer
(light) particles. Attention is drawn to the similarity with Fig. 1.
Reproduced from [390°] with permission.
only weakness to this approach is that the interface
needs to be transferred to a solid substrate by the
Langmuir-Blodgett method. The orogenic mecha-
nism was confirmed in situ by following the displace-
ment of a protein from a solid surface [36'].
In situ measurements on fluid interfaces can be
performed using Brewster angle microscopy (BAM).
Studies by Patino et al. [37,38"] have shown that it is
possible to image interfaces formed by proteins and
surfactants. The surfactants have a high refractive
index compared to the proteins, allowing discrimina-
tion between the two species. They found that mixed
p-casein and monopalmitin films phase separated at
the interface. They also showed an increase in interfa-
cial film thickness. Although BAM has much lower
resolution than AFM, the approaches are highly com-
plimentary, as BAM can observe these phenomena in
situ at the interface.
The orogenic model was further supported in a
separate computer simulation study. By using a Brow-
nian dynamics approach Wijmans and Dickinson
[39"] simulated the competitive displacement process.
The results showed a remarkable similarity to the
experimental observations made using AFM
[33",34'] and BAM [38"], whereby the surfactants
adsorbed and formed distinct domains, compressing
and increasing the thickness of the protein regions.
Fig. 2 shows an example of one of these simulations,
and the likeness between that and Fig. 1 is quite
remarkable. They also support the importance of the
rheology of the protein network in the process, and
also that repulsive forces between the protein and
surfactant promote the phase separation.
180 P.J. Wilde /Current Opinion in ColloidI & Inte8ace Science 5 (2000)176-181
5. Conclusions
Understanding the role of interfaces on the forma-
tion and stability of foams and emulsions has been
significantly advanced in recent years. There appears
to be a consensus of opinion that the surface rheolog-
ical behaviour of both proteins and surfactants is of
paramount importance. However, rheology is a com-
plex area, and the specific surface rheological
parameters, which are most important for these appli-
cations, are still being defined. The main objectives
for the future are to understand how factors such as
molecular structure, component interactions and sur-
face composition of mixed interfaces, influence and
control the various interfacial rheological parameters
which are regarded as important contributory factors
to foam and emulsion behaviour.
Acknowledgements
The author acknowledges the support of the BBSRC
through their core strategic grant to the Institute of
Food Research.
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of special interest
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181
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experimentally. The simulations demonstrated the importance of
the strength of the protein network and showed that repulsive
forces between the protein and surfactants encouraged phase sepa-
ration. This approach should prove to be a powerful tool for
investigating the role of specific inter-molecular interaction
processes on the development of interfacial structure.