Food Hydrocolloids 17 (2003) 25±39

www.elsevier.com/locate/foodhyd
Review

Hydrocolloids at interfaces and the in¯uence on the properties of

dispersed systems q
Eric Dickinson*
Procter Department of Food Science, University of Leeds, Leeds LS2 9JT, UK
Received 20 August 2001; revised 29 October 2001; accepted 16 November 2001

Abstract
Although traditionally associated with thickening and gelation behaviour, food hydrocolloids also in¯uence the properties of dispersed
systems through their interfacial properties. Hence, surface-active hydrocolloids may act as emulsi®ers and emulsion stabilisers through
adsorption of protective layers at oil±water interfaces, and interactions of hydrocolloids with emulsion droplets may affect rheology and
stability with respect to aggregation and serum separation. A review of literature evidence suggests that much of the reported emulsifying
capability of polysaccharides is explicable in terms of complexation or contamination with a small fraction of surface-active protein. To
support this point of view, the speci®c cases of gum arabic, galactomannans and pectin are considered in some detail. In mixed protein 1
polysaccharide systems, associative electrostatic interactions can lead to coacervation or soluble complex formation depending on the nature
of the biopolymers and the solution conditions (pH and ionic strength). Protein±hydrocolloid complexation at interfaces can be associated
with bridging ¯occulation or steric stabilisation. As well as controlling rheology, the presence of a non-adsorbing hydrocolloid can affect
creaming stability by inducing depletion ¯occulation.
q 2002 Elsevier Science Ltd. All rights reserved.
Keywords: Hydrocolloids; Biopolymer emulsi®ers; Surface activity; Emulsion stability; Protein±hydrocolloid interactions; Flocculation

1. Introduction proteins and polysaccharides are compared in Table 1.

Food hydrocolloids are high-molecular-weight hydrophi-
lic biopolymers used as functional ingredients in the food
industry for the control of microstructure, texture, ¯avour
and shelf-life. The term `hydrocolloid' embraces all the
many polysaccharides that are extracted from plants,
seaweeds and microbial sources, as well as gums derived
from plant exudates, and modi®ed biopolymers made by the
chemical or enzymatic treatment of starch or cellulose. In
addition, due to its polydisperse and highly hydrophilic
character, the unique protein gelatin has become accepted
as an exceptional member of this polysaccharide club. But
other food proteins, like casein and gluten, are traditionally
not classi®ed as hydrocolloidsÐeven though they certainly
do exhibit functional properties that overlap considerably
with those of the food polysaccharides.
The general molecular and functional properties of
q
Based on the author's presentation at the Masterclass on `Measuring
Performance' at the 11th Gums and Stabilisers for the Food Industry
Conference (Wrexham, UK, 2±6 July 2001).
* Tel.: 144-1132-332956; fax: 144-1132-332982.
E-mail address: e.dickinson@leeds.ac.uk (E. Dickinson).
0268-005X/03/$ - see front matter q 2002 Elsevier Science Ltd. All rights reserved.
PII: S 0268-005 X(01)00 120-5
Both classes of biopolymer contribute to the structural and
textural properties of foods through their aggregation and
gelation behaviour. Furthermore, proteins are known for
their emulsi®cation and foaming properties, and polysac-
charides for their water-holding and thickening properties.
In reality, of course, Table 1 is a gross simpli®cation. Large
differences in functional properties exist between the
various food biopolymers depending on the detailed chemi-
cal structure and sensitivity to solution conditions (pH, ionic
strength, speci®c ions). The functionality of an individual
biopolymer in foods is also affected by its interactions with
other food componentsÐproteins, polysaccharides, lipids,
sugars, salts, and so forth.
Food colloids are multi-phase food systems containing
particles or other structures with characteristic spatial
dimensions in the colloidal size range (Dickinson, 1992).
The term `colloid' can be applied to particulate dispersions,
foams, gels and emulsions (oil-in-water, water-in-oil, water-
in-water). Therefore, most manufactured foodstuffs can be
classi®ed as food colloids, and many contain hydrocolloid
ingredients added by the manufacturer for control of stabil-
ity and rheological properties. An important class of food
colloids are oil-in-water emulsions such as salad dressing,
26 E. Dickinson / Food Hydrocolloids 17 (2003) 25±39

Table 1 ice-cream, cream liqueurs or soft drinks. The primary stabil-

The common general characteristics and the differences between proteins ising mechanism may occur in the bulk aqueous phase or at
and polysaccharides as functional biopolymers in food systems
the surface of the droplets, depending on the chemical
Similarities nature of the particular ingredient(s) involved (Lips,
Campbell, & Pelan, 1991). In this article, we consider the
Natural polymers
extent to which food hydrocolloids have a role in conferring
Widespread in food colloids
Used in pharmaceuticals, cosmetics, personal products stability on dispersions and emulsions through interfacial
Environmentally friendly polymers action.
Complicated structure In the formulation of emulsion systems, one normally
Complex aggregation behaviour distinguishes between two types of ingredient: the `emulsi-
Gelling/stabilising agents
fying agent' (or `emulsi®er') and the `stabiliser' (Dickinson,
Differences 1992). The emulsifying agent is the single chemical species
(or mixture of species) that promotes emulsion formation
Proteins Polysaccharides and short-term stabilisation by interfacial action. The term
Wide-ranging structures Similar structures
Reactive Unreactive
`bioemulsi®er' (or `biosurfactant') is also commonly used in
Monodisperse Polydisperse the ®eld of biotechnology and applied microbiology
Many segment types Few segment types (Navon-Venezia et al., 1995; Ron & Rosenberg, 2001;
Linear chain Linear or branched Rosenberg & Ron, 1999), although it is rarely used amongst
Flexible chain Stiff chain food technologists (Shepherd, Rockey, Sutherland, &
Medium molecular weight High molecular weight
Small molecular volume Large molecular volume
Roller, 1995).
Amphiphilic Hydrophilic There are two broad classes of emulsifying agents used in
Surface-active Not surface-active food processingÐsmall-molecule surfactants (monoglycer-
Polyelectrolyte Non-ionic or charged ides, polysorbates, sucrose esters, lecithin, etc.) and macro-
Emulsifying/foaming Thickening/waterholding molecular emulsi®ers (usually proteins, especially from
Temperature sensitive a Temperature insensitive
Strong surfactant binding Weak surfactant binding
milk and eggs). A small-molecule surfactant is a distinctly
amphiphilic molecule having both polar and non-polar
a
That is, the structure and properties of most proteins can change dras- parts. For reasons of tradition and marketing, proteins are
tically when heated above a characteristic `denaturation temperature'. not commonly classi®ed as emulsi®ers, even though they do
often operate as such during food manufacture. So, in prac-
tice, the term `emulsi®er' in the food industry is con®ned
almost exclusively to low-molecular-weight amphiphiles.
Confusingly, the term also includes those small molecules
that affect texture or shelf-life in ways other than through
Table 2 emulsi®cation, e.g. by modifying fat crystallisation or by
Principal factors affecting oil-in-water emulsion stability interacting with starch.
To confer substantial shelf-life we require the presence of
Droplet-size distribution
a stabiliser. This can be de®ned (Dickinson, 1992) as a
Initially determined by single chemical component (or mixture) conferring long-term
Emulsi®cation equipment emulsion stability, possibly by an adsorption mechanism,
Concentration of emulsi®er
but not necessarily so. Stabilisers are normally bio-
Type of emulsi®er
Oil/water ratio polymersÐproteins or polysaccharides; small-molecule
Other factors (temperature, pH, viscosity) surfactants are not so effective in conferring long-term
stability. The main stabilising action of food polysacchar-
Nature of interfacial adsorbed layer
ides is via viscosity modi®cation or gelation in the aqueous
Determined by continuous phase. Proteins, on the other hand, have a strong
Concentration and type of emulsi®er tendency to adsorb at oil±water interfaces to form stabilis-
Interactions of adsorbed species ing layers around oil droplets, and so they are able to ful®l
Competition between adsorbed species both the emulsifying and the stabilising roles. Emulsions
Nature of continuous aqueous phase can also be stabilised by particles (e.g. casein micelles and
fat crystals).
Rheology, solvent quality, ionic environment, unadsorbed polymers A stable emulsion is one with no discernible change in the
and amphiphiles
size distribution of the droplets, or their state of aggregation,
Nature of dispersed oil phase or their spatial arrangement within the sample vessel, over
the time-scale of observation. This time-scale may vary
Solid/liquid content from hours to months depending on the situation. The
Solubility in continuous phase
dominant mechanisms of instability are gravity creaming,
 E. Dickinson / Food Hydrocolloids 17 (2003) 25±39
Ostwald ripening, ¯occulation and droplet coalescence
(Dickinson, 1992). Table 2 gives the main factors affecting
stability. The state of ¯occulation of the droplets is depen-
dent on the interactions between stabilising layers, which in
turn depends on factors such as the biopolymer surface
coverage, the layer thickness, the surface charge density,
and the aqueous solution conditions (especially pH, ionic
strength, and divalent ion content). For a freshly prepared
®ne triglyceride oil-in-water emulsion, the most obvious
initial manifestation of instability is creaming, which typi-
cally leads on to macroscopic phase separation into separate
discernible regions of cream and serum. This may then be
followed by droplet coalescence within the cream and
`oiling off' at the top of the sample. All of these processes
can be affected by interactions of the hydrocolloid stabiliser,
both in the bulk aqueous phase and at the surface of the
emulsion droplets.
2. What makes a good emulsifying agent or a good
emulsion stabilising agent?
For a polymer to be effective as an emulsifying agent, it
must be surface-active. That is, it must have the capacity to
lower the tension at the oil±water interface, both substan-
tially and rapidly when present at the concentrations typi-
cally used during emulsi®cation. Generally speaking, the
lower the interfacial tension, the greater the extent to
which droplets can be broken up during intense shearing
or turbulent ¯ow (Walstra, 1983; Walstra & Smulders,
1998). During high-pressure homogenisation, for instance,
most of the processes occur on time-scales of milliseconds
or less: droplet deformation, emulsi®er adsorption, emulsi-
®er spreading, and droplet collision. To retain small droplets
during emulsi®cation, the time between droplet collisions
should be long compared with the time for emulsi®er to
adsorb at the new oil±water interface and to create a tran-
sient stabilising layer (not necessarily with full saturation
coverage). Stabilisation of ®ne oil droplets during emulsi®-
cation can be ascribed predominantly to the Gibbs±Marangoni
mechanism (Dickinson, 1994), which to be effective requires
adsorption of a water-soluble emulsi®er at a suf®cient surface
concentration to generate substantial interfacial tension
gradients during close approach of colliding droplets.
For a biopolymer to be surface-active, it clearly must
have amphiphilic character. So, if it is a hydrocolloid, it
must contain hydrophobic groups that are numerous enough
and suf®ciently accessible on a short timescale to enable the
adsorbing molecules to adhere to and spread out at the inter-
face, thereby protecting the newly formed droplets. The
required time may be too long for very large macromole-
cules, or species that are strongly aggregated in the bulk
aqueous phase. Hence, an ideal emulsifying agent, capable
of making small droplets, is typically composed of species
of relatively low molecular mass with good solubility in the
aqueous continuous phase (e.g. a water-soluble surfactant of
27
high HLB number). The limited emulsifying capacity of
some biopolymers can be attributed to poor solubility and/
or insuf®cient amphiphilic character to produce rapid and
substantial lowering of the interfacial tension during droplet
break-up. The well-established improvement in emulsifying
properties of a protein like gluten by degradative enzyme
treatment (LarreÂ, Huchet, BeÂrot, & Popineau, 2001) can
therefore be attributed to the improved solubility and greater
surfactant-type character of the derived peptide fragments.
Irrespective of the degree of amphiphilic character, though,
the large molecular mass of a typical hydrocolloid makes it
an unlikely candidate for an ingredient of the very highest
emulsifying ability.
One distinctly identi®able group of surface-active poly-
saccharides are the hydrophobically modi®ed cellulose
derivativesÐnotably methylcellulose and hydroxypropyl
methylcellulose. Such amphiphilic biopolymers can cer-
tainly be used as emulsi®ers in their own right to prepare
stable soybean oil-in-water emulsions (Gaonkar, 1991). But
the droplets produced are much coarser than those made
with low-molecular-mass emulsi®ers or proteins under
similar conditions (Darling & Birkett, 1987). This poorer
emulsifying performance is attributable to the relatively
high molecular weight of these modi®ed cellulose polymers.
Similar arguments can be applied in relation to the emulsi-
fying performance of hydrophobically modi®ed starches
and polypropylene glycol alginate.
The reliability of the published literature on the apparent
surface activity of certain hydrocolloids is undermined
somewhat by the fact that many commercial gum samples
contain a small amount of protein, either as contaminant or
as an intrinsic part of the molecular structure. As this pro-
teinaceous material is typically strongly hydrophobic, it can
adsorb strongly at liquid interfaces, thereby giving an erro-
neous impression of the intrinsic surface activity of the
polysaccharide hydrocolloid itself. So, for instance, the
stabilising function of xanthan gum in mayonnaise has
been attributed (Hennock, Rahalkar, & Richmond, 1984)
to its acting as an emulsi®er by co-adsorbing with egg
yolk at the oil±water interface. This interpretation was
argued on the basis that a 1 wt% solution of the gum had
been found (Prud'homme & Long, 1983) to lower the
tension at the air±water surface by 30 mM m 21 or more!
However, it is likely that the gum sample used in the afore-
mentioned research contained as much as 5% of contamin-
ating protein (Anderson, 1986). And it is not only in the `old
literature' that one may ®nd disconcertingly confusing
information. Reports of highly surface-active xanthan
samples still persist in some fairly recent publications
(Garti, Slavin, & Aserin, 1999).
Once an emulsion of small droplets has been successfully
prepared, considerations of surface activity or interfacial
tension gradients are no longer relevant. What matters for
subsequent long-term stability is how well the molecular
characteristics of the adsorbed biopolymer conform to the
requirements of producing a robust macromolecular barrier
28 E. Dickinson / Food Hydrocolloids 17 (2003) 25±39
at the interface. The physico-chemical processes involved in
preventing droplets from aggregating or coalescing are the
classical colloidal stability mechanisms of steric stabilisa-
tion and electrostatic stabilisation (Dickinson, 1988a,b,
1992). For a biopolymer to be most effective in stabilising
dispersed particles or emulsion droplets, it should exhibit
the following four characteristics:
(i) Strong adsorption. This implies that the amphiphilic
polymer has a substantial degree of hydrophobic charac-
ter (e.g. non-polar side chains or a peptide/protein
moiety) to keep it permanently anchored to the interface.
(ii) Complete surface coverage. This implies that there is
suf®cient polymer present to fully saturate the surface.
(iii) Formation of a thick steric stabilising layer. This
implies that the polymer is predominantly hydrophilic
and of high molecular weight (10 4 ±10 6 Da) within an
aqueous medium with good solvent properties.
(iv) Formation of a charged stabilising layer. This
implies the presence of charged groups on the polymer
that contribute to the net repulsive electrostatic inter-
action between particle surfaces, especially at low ionic
strength. (This characteristic is only essential if the poly-
mer layer is not suf®ciently thick.).
Conditions (i)±(iii) cannot be met simultaneously for a
homopolymer in which all the chain segments are chemi-
cally similar, and so such uniform polymers do not make
good steric stabilisers (Dickinson, 1988a). What is needed
for good steric stabilisation is a block copolymer, composed
of a small fraction of strongly adsorbing hydrophobic
segments (to keep the macromolecule permanently attached
to the surface) and a large fraction of non-adsorbing hydro-
philic segments (to stick it away from the surface and confer
upon the protective layer some appreciable thickness). Such
steric stabilisation, combined with electrostatic stabilisation
(i.e. condition (iv)) if the macromolecule contains ionisable
groups, provides a repulsive energy barrier which prevents
pairs of particles from becoming strongly stuck together at
close separations under the strongly attractive in¯uence of
ubiquitous van der Waals forces (Dickinson, 1992).
So, let us turn to four basic questions that lie at the heart
of the subject of this article.
Question 1: Does the hydrophilic character of polysac-
charides mean that they have little surface activity at oil±
water (or air±water) interfaces, and so are not useful as
emulsifying agents? Answer: Yes.
Question 2: Can one say then that hydrocolloids do not
adsorb at surfaces in foods? Answer: Yes, it is true that
hydrocolloids do not normally adsorb at hydrophobic sur-
faces¼but with some exceptions.
Question 3: What are the `exceptions'? Answer: For
instance¼
² gelatin (a protein!).
² gum arabic (contains protein!).
² chemically modi®ed starch or cellulose derivatives (e.g.
highly substituted methyl celluloses).
² some naturally occurring galactomannan hydrocolloids
(e.g. guar gum, fenugreek gum).
² acetylated pectin from sugar beet.
² depolymerised citrus pectin.
² possibly any hydrocolloid adsorbing at a hydrophilic (or
amphiphilic) surface (e.g. at an existing adsorbed protein
layer).
Question 4: Can the reported surface activity and emul-
sifying capability of some carbohydrate polymers be attrib-
uted mainly to the presence of protein, present either as a
contaminant, or as a covalently linked (or physically asso-
ciated) protein±polysaccharide complex? Answer: In most
cases, probably yes.
In order to justify the bare answers given above, it seems
appropriate to discuss a few of the exceptions in more detail.
We shall begin with the most well known of all the food
hydrocolloid emulsi®ersÐgum arabic.
3. Some hydrocolloids with surface activity and
emulsi®cation properties
3.1. Gum arabic
The most commonly recognised hydrocolloid emulsi®er
is gum arabic. It is widely used in the soft drinks industry for
emulsifying ¯avour oils (e.g. orange oil) under acidic condi-
tions. About three-quarters of the gum production comes
from the species Acacia senegal, with Acacia seyal provid-
ing most of the rest (Thevenet, 1988). Gum arabic is the
established benchmark hydrocolloid emulsi®er, and, because
it is a fairly expensive ingredient, there have been many
suggestions in the literature for its replacement by other
polymeric emulsi®ersÐlike hydrophobically modi®ed
starch (Trubiano, 1995) or other gums, e.g. mesquite gum
(Vernon-Carter, 1998).
The well-known ®lm-forming ability of gum arabic has
long since unambiguously established that this is indeed a
genuine emulsi®er that confers functionality not by modify-
ing the rheology of the aqueous phase but by leading to
formation of a macromolecular stabilising layer around oil
droplets. Hence, the gum can stabilise the ¯avour oil emul-
sion both as a concentrate and in the form of a diluted
(carbonated) beverage (Tan, 1990). Nevertheless, the level
of surface activity is actually rather low in comparison with
typical food protein emulsi®ers. To compensate for this in
generating stable sub-micron-sized droplets, it is necessary
in practice (McNamee, O'Riordan, & O'Sullivan, 1998) to
use a rather high gum-to-oil weight ratio, i.e. approximately
1:1, as compared with 1:10 for equivalent protein-stabilised
emulsions. Once formed by adsorption at a macroscopic
oil±water interface, the high surface shear viscosity of the
gum arabic ®lm is little affected by extensive dilution of the
 E. Dickinson / Food Hydrocolloids 17 (2003) 25±39
Fig. 1. Schematic representation of the wattle blossom model representing
the functionally active component of A. senegal gum (a) in solution and (b)
adsorbed at the oil±water interface. Separate hydrophilic carbohydrate
blocks (C) of molecular mass ca. 2 £ 105 Da are attached to the backbone
chain of hydrophobic protein (P).
aqueous sub-phase (Dickinson, Elverson, & Murray, 1989).
The ®lm viscoelasticity is therefore maintained even when a
major proportion of the hydrocolloid has been removed
from the aqueous phase in contact with the adsorbed
layer. This is consistent with the observation that only a
small proportion of gum arabic used in emulsion preparation
is actually involved in the stabilisation process.
Gum arabic (A. senegal) is a complex branched hetero-
polyelectrolyte with a backbone of 1,3-linked b-galactopyr-
anose units and side-chains of 1,6-linked galactopyranose
units terminating in glucuronic acid or 4-O-methylglucuro-
nic acid residues. It also contains ca. 2% protein, covalently
linked to carbohydrate through serine and hydroxyproline
residues, resulting in a mixture of arabinogalactan±protein
complexes, each containing several polysaccharide units
linked to a common protein core. This so-called `wattle
blossom' model (Connolly, Fenyo, & Vandevelde, 1988;
Fincher, Stone, & Clark, 1983) is shown schematically in
Fig. 1(a). It has been demonstrated that the gum is a
complex mixture of at least three distinct fractions with
different chemical structures (Williams, Phillips, & Randall,
1990) with a major component containing little or no pro-
teinaceous material. The protein element appears to be
mainly associated with a high-molecular-mass fraction
representing less than 30% of the total gum (Vandevelde
& Fenyo, 1985). It is this fraction that appears to be pre-
dominantly responsible for the special emulsifying and
stabilising properties of the hydrocolloid (Randall, Phillips,
& Williams, 1988; Ray, Bird, Iacobucci, & Clark, 1995).
Such heterogeneity of macromolecular structure and func-
tionality is by no means unique to gum arabic. Molecular
weight fractions with differing emulsi®cation properties
29
have also been identi®ed for other gums, e.g. gum talha
(Underwood & Cheetham, 1994).
Fig. 1(b) shows the high-molecular-mass protein-rich frac-
tion of A. senegal gum adsorbing at the oil±water interface
according to the wattle blossom representation (Islam,
Phillips, Sljivo, Snowden, & Williams, 1997; Randall,
Phillips, & Williams, 1989). The more hydrophobic protein
chain ®rmly anchors the protein±polysaccharide hybrid at the
interface, and the protruding hydrophilic carbohydrate blocks
attached to this chain provide a strong steric barrier towards
¯occulation and coalescence. Whilst charged groups provide
the basis for some electrostatic contribution to the colloidal
stabilisation, the relatively low value of the (negative) zeta
potential, 10±20 mV under beverage emulsion conditions
(Jayme, Dunstan, & Gee, 1999; Ray et al., 1995), indicates
that the primary stabilisation mechanism is steric in character.
Reports of the surface activity of various Acacia gums with
nitrogen contents in the range 0.1±7.5% (Dickinson, Murray,
Stainsby, & Anderson, 1988) suggest a good correlation
between the Acacia gum protein content and the limiting
long-time interfacial tension, and also between emulsifying
capacity and the initial rate of change of tension with time.
Consistent with this generalisation, A. senegal ®lms have been
found to be more elastic and of higher stability than those
composed of A. seyal (Fauconnier et al., 2000). Notwithstand-
ing that, nitrogen content alone is really no reliable indicator
of the effectiveness of Acacia gums for emulsi®cation. Gum
arabic (A. senegal) samples of similar nitrogen content
(,0.3%, i.e. corresponding to ,2% protein) have been
found (Dickinson, Galazka, & Anderson, 1991a) to exhibit
substantial differences in emulsifying capacity and emulsion
stability. Furthermore, some samples of A. seyal, having a
considerably lower protein content (,0.8%), have actually
been found to give better emulsion stability than A. senegal
(Buffo, Reineccius, & Oehlert, 2001).
On the other hand, there does appear to be a good correla-
tion between emulsion stability and gum arabic average
molecular weight. It was observed (Dickinson, Galazka, &
Anderson, 1991b) that the 10% fraction of a gum arabic
sample corresponding to the highest molecular weight
(0.38% N), as separated by gel permeation chromatography,
could produce a more stable emulsion than the remaining
90% fraction (0.35% N). Additionally, in separate experi-
ments, when the average molecular mass of a gum arabic
sample (,0.35% N) was gradually reduced from 3:1 £ 105
to 2:2 £ 105 Da by controlled irradiative degradation, the
resulting emulsion stability was correspondingly reduced
(Dickinson, Galazka, & Anderson, 1991c). This trend is
consistent with the formation of thicker and more effective
steric stabilising layers by adsorption of polymers of greater
molecular mass.
3.2. Galactomannans
A galactomannan is a rather rigid hydrophilic biopolymer
with a polymannose backbone and grafted galactose units.
30 E. Dickinson / Food Hydrocolloids 17 (2003) 25±39
Fig. 2. Comparison of the emulsion stabilising ability of depolymerised
citrus pectin fractions (70% DE) with that of gum arabic (GA) (Akhtar et
al., 2002). Fine emulsions were prepared by high-pressure homogenisation
of 10% rapeseed oil and 4 wt% hydrocolloid at pH 4.7 and ionic strength
0.2 M. Percentage serum separation is shown for four pectin samples with
different degrees of depolymerisation (different values of average molecu-
lar mass, in Da) after 1 month (A), 2 months and 3 months (B).
Galactomannans such as guar and locust bean gum are
widely used in the food industry as thickening, water-
holding and stabilising agents. As the carbohydrate structure
gives no suggestion of the presence of any signi®cant
proportion of hydrophobic groups, it is generally assumed
that this type of hydrocolloid functions by modifying the
rheological properties of the aqueous phase between the
dispersed particles or droplets.
Puri®ed guar or locust bean gum is reported not to exhibit
any surface activity (Gaonkar, 1991). Nevertheless, there
are some statements in the literature (Garti, 1999, 2001;
Garti & Reichman, 1993, 1994) that these polymers have
the capacity to emulsify oils and stabilise fairly coarse emul-
sions (,10 mm mean droplet size, 3±4 mg m 22 surface
coverage) at a moderately low gum/oil ratio (say, 1:5). It
has been suggested by Garti and Reichman (1994), based on
light microscopy observations of strong birefringency at the
oil±water interface, that these gums stabilise emulsions by
forming liquid crystalline layers around the droplets. We are
reminded here of the suggestion of Friberg (1971) concern-
ing the stabilising role of small-molecule emulsi®ers by
multi-layer lamellar liquid crystals. Nevertheless, it has
been commented upon before (BergenstaÊhl, 1997; Dickinson,
1986) that the applicability of this stabilisation mechanism
to food emulsions is likely to be limited in practice.
A lowering of the interfacial tension by guar and locust
bean gums by up to ca. 20 mM m 21 has been reported
(Garti, 1999; Garti & Reichman, 1994). While these authors
are genuinely convinced that this surface activity is an
intrinsic property of the polysaccharide itself, and not due
to the presence of contaminating protein, it is fair to say that
all such samples probably do contain a residual strongly
bound protein/peptide fraction, which is likely to be the
origin of much of the apparent emulsifying functionality
of galactomannan gums. Based on a study of 10 commercial
samples, Anderson (1986) reported an average nitrogen
content of 0.57% for guar gum. This corresponds to
,2.5% protein, which is actually higher than typically
found for gum arabic! Garti and Reichman (1994) puri®ed
their guar gum down to 0.8% protein, but still found a simi-
lar degree of surface activity and emulsi®cation ability.
Hence, based on this evidence, it is conceivable that this
polysaccharide may confer some emulsion stabilising
property in its own right bound to the interface through
the slight hydrophobicity of the polymannose backbone.
Even if this is the case, however, it should be noted that
this putative adsorption of the gum to the oil±water inter-
face is reportedly rather weak and reversible. That is, the
birefringency around the droplets and the associated emul-
sion stability is lost on diluting the aqueous phase of the
emulsion with water (Garti & Reichman, 1994).
Another galactomannan that has received particular
attention recently is fenugreek gum. Garti, Madar, Aserin,
and Sternheim (1997) have reported that puri®ed fenugreek
gum has substantial surface activity and that stable emul-
sions of moderately low average droplet size (,3 mm) can
be produced; moreover, physical separation of the con-
taminating protein from the crude gum material did not
apparently reduce the measured surface activity. Con-
versely, however, in a separate recent study (Brummer,
Cui, & Wang, 2001) where a fenugreek gum sample
containing 2.4% protein was enzymatically treated with
pronase, the ability of the resulting hydrolyzate (containing
0.6% protein, but of the same overall molecular weight) was
found to be substantially reduced. It can therefore be reason-
ably inferred that the surface activity of fenegreek gum, like
that of gum arabic, is due to the presence of a small fraction
of protein closely associated (chemically or physically) with
the polysaccharide structure.
3.3. Pectin
Pectins extracted from plant cell walls are commonly
used as a gelling and thickening agent in foods. High meth-
oxyl pectin ($50% DE) forms gels under acidic conditions
in aqueous media of high sugar content, whereas low meth-
oxyl pectin forms gels in the presence of calcium ions.
Typically, commercial pectins extracted from citrus peel
or apple pomace are not effective as emulsifying agents
irrespective of the degree of esteri®cation. There are, how-
ever, some exceptions to this statement.
Highly acetylated pectin from sugar beet has been
reported (Dea & Madden, 1986) to be much more surface-
active than commercial high-methoxyl or low-methoxyl
pectins, and hence to be readily capable of producing and
stabilising ®ne vegetable oil-in-water emulsions. According
to Dea and Madden (1986), the molecular origin of the
considerable emulsifying capacity of sugar beet pectin is
the substantially hydrophobic character of the acetyl groups
(2±9%). Nevertheless, it should be noted that the experi-
ments upon which this statement was based were carried out
on samples containing .2 wt% protein.
Even with a low acetyl content (,0.8%), pectins from
citrus fruits and apples can also exhibit good surface activity
 E. Dickinson / Food Hydrocolloids 17 (2003) 25±39
and emulsion stabilising characteristics if the average
molecular weight is reduced to ,80 kDa by severe acid
hydrolysis (Mazoyer, Leroux, & Bruneau, 1999). Based
on time-dependent changes in emulsion droplet-size distri-
bution and serum separation, depolymerised pectin of mole-
cular weight 70 kDa and 70% degree of esteri®cation has
been used to make highly stable ®ne oil-in-water emulsions
at a relatively low gum/oil ratio (1:5) (Akhtar, Dickinson,
Mazoyer, & Langendorff, 2002). Emulsion stability was
found to be reduced on increasing the pH from 4.7 to 7,
or by substantially increasing (or decreasing) the pectin
molecular weight (Fig. 2).
Independent of the amount of depolymerised pectin used,
the proportion of the hydrocolloid adsorbed at the oil±water
interface during emulsi®cation was found to remain roughly
constant at ca. 25% (Akhtar et al., 2002). The aqueous
phases of the original pectin solutions, and the serum layers
of the emulsions separated by centrifugation, were both
analysed with respect to protein content. This showed that
a negligible proportion of the original protein content of the
sample (0.6 wt%) was detectable in the aqueous phase after
emulsi®cation. Thus, it appears that the protein fraction of
the hydrocolloid emulsi®er was almost entirely associated
with the adsorbed layer around the droplets. Furthermore,
the fraction remaining in the serum phase was found to be
quite ineffective for subsequent emulsi®cation. We there-
fore can infer that the presence of the protein moiety in
the depolymerised pectin plays a major functional role in
enhancing the emulsi®cation properties of pectin following
depolymerisation. The analogy with gum arabic is again
quite noteworthy. That is, the hydrophobic protein com-
ponent is responsible for the surface activity of the hydro-
colloid emulsi®er, acting as the strong anchor point at the
oil±water interface, with the hydrophilic polysaccharide
chains providing the protective layer that confers effective
steric stabilisation during extended storage.
4. Interactions of hydrocolloids with proteins
4.1. Interactions in aqueous solution
The nature and strength of protein±hydrocolloid inter-
actions in bulk solution and at interfaces have an important
in¯uence on the stability properties of food dispersions and
emulsions (Dickinson, 1993; Dickinson & Euston, 1991). In
aqueous solution, a binary mixture of protein 1 hydro-
colloid can exhibit one of three different equilibrium situa-
tions (Albertsson, 1971): (a) miscibility, (b) thermodynamic
incompatibility, and (c) complex coacervation (or com-
plexation). Miscibility occurs commonly at low biopolymer
concentrations, and either incompatibility or coacervation at
high concentrations, depending on whether the protein±
hydrocolloid interaction is net repulsive or net attractive,
respectively. Thermodynamic incompatibility implies the
separation into two distinct aqueous phases, one rich in
31
protein and the other rich in hydrocolloid. Two distinct
phases also arise in complex coacervation, except that
now one phase is rich in the two biopolymers and the
other phase is depleted in both.
A useful parameter to quantify the relative strength of the
binary protein±hydrocolloid interaction in dilute solution is
the cross second virial coef®cient (Ap±h) as may be deter-
mined experimentally by static light scattering from a poly-
mer mixture (Kaddur & Strazielle, 1986). Positive and
negative values of Ap±h are indicative of net repulsive and
net attractive interactions, respectively. The overall thermo-
dynamic behaviour of the mixed bipolymer solution
depends on the relative values of Ap±h, Ap±p and Ah±h,
where Ap±p and Ah±h are the pure protein and pure hydro-
colloid virial coef®cients, representing the contributions
from protein±protein and hydrocolloid±hydrocolloid inter-
actions, respectively. The low polymeric entropy of mixing
means that, if the protein±hydrocolloid interaction is only
slightly net repulsive (i.e. Ap±h . …Ap±p £ Ah±h †1=2 ), the
system prefers to exist as two separate phases when the
overall biopolymer concentration reaches just a few percent
(Grinberg & Tolstoguzov, 1997). Values of Ap±h for many
combinations of food proteins and hydrocolloids are such
that the system exhibits thermodynamic incompatibility.
There are only a very few casesÐe.g. serum albumin 1
pectin (Semenova, Bolotina, & Dmitrochenko, 1991)Ðfor
which genuinely complete miscibility has been established
in the non-dilute mixed biopolymer solution. The rest exhi-
bit some kind of soluble complexation, complex coacerva-
tion or amorphous co-precipitation, depending on the
biopolymer structures involved and the solution conditions
(pH, ionic strength, etc.). At one extreme, with weak or
speci®c unlike attractive interactions …Ap±h , 0†; we may
have a one-phase non-ideal dilute solution of soluble
mixed complexes; and at the other extreme, with strong
unlike attractions …Ap±h p 0† and stoichiometric release of
microions, we may get a mixed precipitate formed with very
little water present. Strictly speaking, complex coacervation
represents the middle ground of a separated liquid-like
phase of mixed biopolymers, which are strongly hydrated
and osmotically swelled, for the retention of microions
(Dubin, 2001).
Unless protein and hydrocolloid carry opposite net
charges, complex coacervation generally does not take
place. The phenomenon tends to be suppressed also at low
biopolymer charge densities. Precipitation and/or gelation
may occur at high charge densities. The maximum coacer-
vation yield occurs for the case of an equal ratio mixture (by
weight) of biopolymers at the pH where they carry equal and
opposite charges (Schmitt, Sanchez, Desobry-Banon, &
Hardy, 1998). The extent to which a particular biopolymer
is involved in Coulombic interactions depends on how far
its isoelectric point pI differs from the solution pH. Most
food proteins …pIp , 5† form complex coacervates with
anionic hydrocolloids …pIh , 3† in the intermediate region
of pH where the two macromolecules carry opposite net
32 E. Dickinson / Food Hydrocolloids 17 (2003) 25±39
Fig. 3. Distribution of charge on the surface of bovine serum albumin
(BSA) at pH 7 as calculated by Hattori et al. (2001). Pictures (a)±(c)
show the protein molecule viewed from three different directions. Surface
regions coloured red and blue carry local net negative and net positive
charges, respectively, and white regions are locally electrically neutral.
(Reproduced with permission from Hattori et al., (2001)).
charges …pIp , pH , pIh †: According to Ledward (1994),
the strength of complexation between protein and polysac-
charide depends on the distribution of ionisable groups on
the surface of the protein, the ease of unfolding of the
protein's native structure, and the backbone ¯exibility and
charge distribution on the polysaccharide. The extent of
reversibility of complexation depends on the aqueous
environment and on the mixing conditions (Tolstoguzov,
1986). The tendency towards the non-equilibrium formation
of an insoluble coacervate is enhanced at low salt concen-
trations and at pH values signi®cantly below pIp.
When both biopolymers carry a net negative charge,
soluble complexes may be produced (Dickinson, 1995b).
In this case, any electrostatic interaction involves the anio-
nic polyelectrolyte interacting with positively charged local
patches on the protein (Park, Muhoberac, Dubin, & Xia,
1992). The importance of such charged patches has long
been recognised in protein chromatography (Regnier,
1987). Increasing the net negative charge on the protein
has two effects: (a) it enhances protein±protein electrostatic
repulsion (i.e. it increases Ap±p) and (b) it reduces protein±
hydrocolloid attraction by screening the interactions of posi-
tively charged groups (i.e. it increases Ap±h). The positively
charged groups on a protein (±NH31) interact more strongly
with ±OSO32 groups than with 2CO22 groups. This means
that, in terms of the relative contributions of effects (a) and
(b), a useful distinction can be made between a sulfated
hydrocolloid like carrageenan and a carboxylated hydrocol-
loid like pectin. At low ionic strength, sulfated hydrocol-
loids of relatively high charged density form fairly strong
reversible complexes with proteins, even at neutral or alka-
line pH (i.e. well above pIp). In contrast, at pH . pIp ; any
interaction of a protein with a carboxylated hydrocolloid
interaction is quite weak or non-existentÐor the system
may even exhibit thermodynamic incompatibility.
Computer modelling of the electrostatic binding of
human serum albumin (HSA) to the strongly anionic poly-
saccharide hyaluronic acid (HA) has recently been reported
(GrymonpreÂ, Staggemeier, Dubin, & Mattison, 2001).
Under incipient binding conditions …pH . pIp †; these calcu-
lations reveal a region of positive electric potential 0.5 nm
from the protein's van der Waals surface. This charged
domain diminishes in intensity with increasing pH or
ionic strength, and its size and curvature are such that it
can readily accommodate a 12 nm long section of the poly-
electrolyte. The electrostatic interaction energy of the
HSA±HA complex under such incipient binding conditions
has been estimated as ca. 1 kT (Grymonpre et al., 2001).
Fig. 3 shows the calculated charge density distribution on
the surface of bovine serum albumin (BSA) as viewed from
three different directions (Hattori, Kimura, Seyrek, &
Dubin, 2001). Although the protein carries a net negative
charge, there is a clearly de®ned patch (size 2±3 nm) of
positive charge on the BSA molecule surface even at pH
7. Involvement of this patch in electrostatic binding at pH .
pIp allows BSA to form soluble complexes at low ionic
strength with dextran sulfate, i-carrageenan and k-carrageenan.
The electrostatic character of the complexes has been
demonstrated (Galazka, Smith, Ledward, & Dickinson,
1999) by their reversible dissociation in the presence of
added electrolyte (0.02±0.1 M NaCl). At low ionic strength,
the `critical' upper pH for effective complexation with BSA
is ca. 6.5 for k-carrageenan, as compared with ca. 7 for i-
carrageenan, and .7 for dextran sulfate. The value of the
protein net charge at the critical pH for complexation has
been shown (Mattison, Dubin, & Brittain, 1998) to be
proportional to the square root of ionic strength, and to
depend on polyelectrolyte charge density (Dickinson,
1998). With respect to adjustment of pH or ionic strength,
the relative strengths of the BSA±polysaccharide inter-
actions correlate well with the relative densities of charged
groups along the different polysaccharide chains: dextran
sulfate . i-carrageenan . k-carrageenan.
An extreme type of protein±polysaccharide interaction
occurs when a covalent linkage is formed between the two
kinds of biopolymers (Dickinson, 1993). The motivation to
construct such a mixed biopolymer conjugate might be the
attempt to generate a new type of `natural' amphiphilic
hydrocolloid having emulsi®cation properties as good as
or better than gum arabic. Without using any chemicals,
covalent protein±polysaccharide conjugates can be prepared
 E. Dickinson / Food Hydrocolloids 17 (2003) 25±39
Fig. 4. Schematic representation of three alternative effects of the adsorp-
tion of stiff hydrocolloid polymers on the surface of spherical emulsion
droplets depending on the hydrocolloid concentration and the nature of
the hydrocolloid±protein interaction: (a) a sterically stabilised system, (b)
an emulsion gel, and (c) a system ¯occulated by macromolecular bridging.
Fig. 5. In¯uence of i-carrageenan on the state of ¯occulation of BSA-stabi-
lised emulsions (20 vol% oil, 1.7 wt% protein, pH 6, ionic strength
0.005 M) stored at 25 8C for 40 h. The average apparent droplet size d32
is plotted against the hydrocolloid concentration ch added to the freshly
made emulsion. (Reproduced with permission from Dickinson and
Pawlowsky (1997)).
33
by linking protein 1-amino-groups to the reducing-end
carbonyl groups of polysaccharides through controlled
Maillard reaction (Kato, Sasaki, Furuta, & Kobayashi,
1990). For instance, the slow dry heating of mixtures of
b-lactoglobulin 1 dextran produces soluble conjugates
with substantially improved solubility and emulsifying
properties compared to the protein alone (Dickinson &
Galazka, 1991). From the hydrocolloid functionality point
of view, a major advantage of covalent bonding over
electrostatic protein±polysaccharide complexation is the
maintenance of a strong association over a wide range of
pH and ionic strength without any incipient coacervation or
precipitation. So, in contrast to casein, which starts to preci-
pitate below pH < 5:5; a casein±maltodextrin conjugate
can be prepared (Shepherd, Robertson, & Ofman, 2000)
which has good solubility and is an effective emulsi®er
under acidic conditions.
4.2. Interactions of hydrocolloids with adsorbed protein
layers
Some food hydrocolloids achieve interfacial functionality
in emulsions, not so much by adsorbing directly at the oil±
water interface during emulsi®cation, but rather by forming
an associative interaction after emulsion formation with the
stabilising protein layer. Partial unfolding of globular
proteins may make them more susceptible to complexation
with hydrocolloids in the adsorbed state than in aqueous
solution at the same pH and ionic strength (Dickinson,
1995a). Rather direct evidence for protein±polysaccharide
complexation at the oil±water interface is provided by
surface shear rheology measurements, e.g. for BSA 1
dextran sulfate at neutral pH (Dickinson & Galazka,
1992), and by particle electrophoretic mobility measure-
ments, e.g. for BSA 1 sodium alginate below neutral pH
(Ward-Smith, Hey, & Mitchell, 1994). More indirect
evidence for interfacial complexation comes from bulk
rheological and ¯occulation studies of emulsions.
Strong attractive interaction …Ap±h p 0† between
adsorbed protein and hydrocolloid present at suf®ciently
high total concentration typically produces a secondary
layer of steric stabilising polymer around protein-coated
emulsion droplets (see Fig. 4(a)). At an excess hydrocolloid
concentration high enough to cause gelation in the aqueous
phase, the hydrocolloid-coated droplets may become immo-
bilised in the polymer gel network (Fig. 4(b)) leading to
increased stabilisation (an emulsion gel). Conversely, the
same protein-coated emulsion droplets may become
destabilised by bridging ¯occulation (Fig. 4(c)) if the hydro-
colloid±protein association is weak …Ap±h , 0†; or if the
hydrocolloid is not present at high enough total concentra-
tion to saturate all the surfaces of the droplets. Bridging
¯occulation of emulsion droplets may also be induced by
adhesion of oppositely charged colloidal particles or even
bacterial cells (Li, McClements, & McLandsborough,
2001).
34 E. Dickinson / Food Hydrocolloids 17 (2003) 25±39
Fig. 6. In¯uence of high-methoxyl pectin on the rheology of pure casein-
stabilised emulsions (40 vol% oil, 2 wt% protein, pH 5.5, ionic strength
0.01 M). The limiting zero-shear-rate viscosity at 22 8C is plotted against
hydrocolloid concentration for emulsions made separately with as1-casein
(W) and b-casein (X). (After Dickinson et al. (1998)).
Bridging ¯occulation of a BSA-stabilised emulsion has
been found to be induced by addition of i-carrageenan under
conditions of soluble complex formation in aqueous solu-
tion (Dickinson & Pawlowsky, 1997). Fig. 5 shows the
effect of added hydrocolloid concentration ch on the average
apparent particle size d32 of a BSA-stabilised emulsion with
an aqueous phase of pH 6 and low ionic strength. In the
emulsion sample without added hydrocolloid, or in samples
with ch # 1023 wt%, the low value of d32 < 0:5 mm corre-
sponds to the actual sizes of individual dispersed droplets.
However, for ch $ 5 £ 1023 wt%, there is a jump in the
apparent particle size by more than an order of magnitude
due to bridging ¯occulation of the BSA-coated droplets by
i-carrageenan. This high value of d32 < 10 mm is a rough
measure of the average ¯oc size in emulsions with hydro-
colloid added in the concentration range 0.01±0.1 wt%.
Partial restabilisation at higher i-carrageenan contents is
indicated by the considerably reduced values of d32 for
ch . 0:1 wt%. At this ionic strength (0.005 M), changing
the aqueous phase conditions to pH 7 leads to a protein±
hydrocolloid interaction that is too weak to induce
signi®cant ¯occulation (Dickinson & Pawlowsky, 1996).
However, upon addition of the more highly charged (and
therefore more strongly protein-associating) dextran sulfate
instead of i-carrageenan, substantial bridging ¯occulation
was found to occur at pH 7 (and higher).
Protein±polyelectrolyte interactions are sensitive to
details of protein structure as well as to the charge density
on the polyelectrolyte. For instance, in distinct contrast to
the behaviour of BSA, the globular protein b-lactoglobulin
(with a similar pIp) shows little evidence of signi®cant
electrostatic complexation with dextran sulfate at neutral
pH and low ionic strength, based on measurements of the
electrophoretic mobility of the protein-coated droplets
(Dickinson, 1995a,b). Furthermore, again in contrast to
BSA, the same polyelectrolyte appears to cause no discern-
ible bridging ¯occulation of b-lactoglobulin-stabilised
emulsions or enhancement of protein layer surface shear
viscosity at the oil±water interface.
High-methoxyl pectin adsorbs on the surface of casein-
coated oil droplets and stabilises them under pH conditions
where the precipitation of the emulsions would otherwise
take place (Dalgleish & Hollocou, 1997). Even though the
attractive interaction of carboxylated hydrocolloid with
adsorbed protein may be quite weak at pH . pIp ; it can
nonetheless have a substantial in¯uence on the stability
and rheology of a concentrated emulsion. This has been
illustrated (Dickinson, Semenova, Antipova, & Pelan,
1998) for the case of as1-casein-stabilised emulsions
containing high-methoxyl pectin at pH 5.5 and low ionic
strength. The very high bulk viscosity of these ¯occulated
emulsions for ch $ 1 wt% (see Fig. 6) is attributable to
signi®cant attractive protein±polysaccharide interaction at
the surface of the droplets. Associative interfacial inter-
action has been con®rmed at the macroscopic oil±water
interface by a ®ve-fold increase in the surface shear viscos-
ity of an adsorbed as1-casein layer on introducing pectin into
the aqueous sub-phase. This behaviour is thermodynami-
cally consistent with the negative cross second virial coef®-
cient Ap±h derived from light scattering for an aqueous
solution of as1-casein 1 pectin at pH 5.5 and ionic
strength 0.01 M (Semenova et al., 1999). In contrast, the
value of Ap±h is positive for the equivalent aqueous solution
of b-casein 1 pectin, and the viscosity of the (non-¯occu-
lated) pectin-containing b-casein-stabilised emulsion is
very much lower than that of the equivalent as1-casein
system, as shown in Fig. 6.
With certain hydrocolloids, interfacial complexation is
more likely to have its origin in hydrogen bonding rather
than in electrostatic interactions. This seems especially the
case with the uniquely hydrophilic protein gelatin which has
the ability to form gel-like layers at a range of different
surfaces (Izmailova et al., 2001). In particular, a thin layer
of gelatin network may accumulate at a surface already
coated with another more surface-active biopolymer.
Consider, for example, the mixed system of b-casein
(pI < 5) 1 acid processed type-A gelatin (pI < 9) at neutral
pH. Whereas surface tension experiments indicate that the
primary interfacial layer is totally dominated by the much
more surface-active b-casein, measurements of surface
shear viscosity are at least an order of magnitude higher
for b-casein 1 gelatin than for b-casein alone, indicating
the presence of a considerable amount of gelatin at the
interfacial region (Galazka & Dickinson, 1995). Due to
the opposite net charges of the two biopolymers, the
association between molecules in primary and secondary
layers could reasonably be interpreted solely in terms of
electrostatic interaction. However, there is separate
evidence available (Castle, Dickinson, Murray, & Stainsby,
1987) of accumulation of secondary layers of negatively
charged alkali-processed type-B gelatin …pI < 5† below
a primary layer of negatively charged casein at neutral
pH, again based on surface shear viscometry, but in
 E. Dickinson / Food Hydrocolloids 17 (2003) 25±39
Fig. 7. In¯uence of xanthan gum on the creaming of sodium caseinate-
stabilised emulsions (10 wt% oil, 0.5 wt% protein, pH 7, ionic strength
0.005 M) stored at 25 8C in 10 cm tubes. The serum layer height H is
plotted against the storage time t for various concentrations of hydrocolloid
added to the freshly made emulsion: P, 0 wt% and $0.125 wt%; V,
0.025 wt%; W, 0.05 wt%; L, 0.0625 wt%; O, 0.1 wt%. (Reproduced with
permission from Cao et al., (1990)).
this case with sodium caseinate instead of b-casein. Gela-
tin is well known for its thermoreversible gelation via
cooperative hydrogen-bonded interactions within the
collagen-type helices that are essential in providing
cross-links (Izmailova et al., 2001). Hence, it would
appear reasonable to speculate that such cooperative
intermolecular hydrogen-bonding forces, probably supple-
mented by attractive ionic forces, are mainly responsible
for holding together the mixed casein/gelatin interfacial
®lm.
Thermal or hydrostatic pressure processing of a protein-
stabilised emulsion, which induces changes in globular
protein structure, can also in¯uence protein±hydrocolloid
interactions at the surface of protein-coated droplets,
with signi®cant implications for stability and rheology.
Substantial effects of high-pressure treatment on emulsion
properties have recently been found for systems containing
b-lactoglobulin 1 low methoxy pectin (Dickinson & James,
2000) and ovalbumin 1 sulfated polysaccharides (Galazka,
Dickinson, & Ledward, 2000). Following partial denatura-
tion, the number of available interacting sites on the protein
increases as buried groups are liberated (Ledward, 1994).
As well as inducing unfolding of the globular proteins, the
application of high hydrostatic pressure (a few kilobars)
leads to disruption of intermolecular ionic bonds and
hence to dissociation of electrostatic complexes. When pres-
sure is released, the ionic attractive interactions are restored,
and rapid recomplexation of it occurs, but now between the
polysaccharide and the partly denatured protein (Galazka,
Ledward, Sumner, & Dickinson, 1997). The greater mole-
cular ¯exibility of the denatured state allows con®gurational
adjustments to occur which maximise favourable ionic
interactions resulting in more stable complexes than with
the native protein.
35
5. Effect of non-adsorbing hydrocolloids on colloidal
stability
For completeness in this review, it is appropriate to
consider the in¯uence of non-adsorbing hydrocolloids on
the stability of food colloids. Like surfactant micelles or
even unadsorbed milk proteins, hydrocolloids located in
the aqueous phase can induce the destabilisation of disper-
sions and emulsions by the mechanism of depletion ¯occu-
lation (Dickinson, 1995b; Dickinson & Euston, 1991). This
arises when pairs of particle surfaces approach within a
distance less than the mean diameter of the free polymer
molecule in aqueous solution. The exclusion of the polymer
from the intervening gap is associated with an attractive
interparticle force, resulting from the tendency of solvent
to ¯ow out from the gap under the in¯uence of the local
osmotic pressure gradient (Napper, 1983). At very low
concentrations of free polymer, the entropy loss linked to
particle aggregation outweighs the depletion effect and the
system remains stable. However, beyond a certain critical
polymer concentration, which decreases with increasing
particle volume fraction and increasing molecular mass of
the polymer, reversible depletion ¯occulation occurs, lead-
ing to enhanced sedimentation and phase separation. Hence,
a concentrated protein-stabilised emulsion is highly suscep-
tible to destabilisation by depletion ¯occulation following
addition of a small amount of non-adsorbing hydrocolloid
…Ap±h . 0†: The emulsion destabilisation is manifest in rapid
creaming and serum separation (Dickinson, 1993). Hydro-
colloids inducing strong depletion ¯occulation, however,
may produce apparent restabilisation with respect to
serum separation due to the formation of a long-lasting
gel-like network of aggregated droplets (Parker, Gunning,
Ng, & Robins, 1995).
For non-adsorbing macromolecular species present at
®xed volume fraction, it has been shown theoretically
(Piech & Walz, 2000) that the magnitude of the depletion
attraction energy between particles increases with the
degree of non-sphericity of the macromolecular species.
Hence, non-adsorbing hydrocolloids with extended and
stiff polysaccharide backbones are especially effective at
inducing depletion ¯occulation. This is shown in Fig. 7
for the case of xanthan gum added at various low concen-
trations to a model protein-stabilised emulsion system
(10 vol% oil) of sample height 10 cm. The kinetics of
destabilisation is indicated by plotting serum layer thickness
against storage time. The reference emulsion (no added
hydrocolloid) shows no serum separation discernible by
eye during storage at 25 8C for three days (Cao, Dickinson,
& Wedlock, 1990). The presence of a very low concentra-
tion of xanthan (0.025 or 0.05 wt%) is enough to induce
depletion ¯occulation, leading to rapid separation (complete
within 1±2 h) of the low-viscosity liquid-like emulsion to
form a 65±70% serum layer. The same degree of phase
separation takes about two days to complete at 0.0625 wt%
xanthan. Furthermore, there is only ,10% serum separation
36 E. Dickinson / Food Hydrocolloids 17 (2003) 25±39
Fig. 8. Rheology of small-molecule surfactant-stabilised emulsions
(30 wt% oil, 1 wt% surfactant, pH 7, ionic strength 0.05 M) containing
0.1 wt% rhamsan gum incorporated after emulsi®cation. The apparent
shear viscosity h at 25 8C is plotted against the shear stress S on a log±
log scale for two different surfactants as emulsifying agent: W, Tween 20;
X, SDS. (Reproduced with permission from Dickinson et al. (1993)).
after three days in the presence of 0.1 wt% xanthan, and
none at all after three days at 0.125 wt% xanthan. Stability
towards cream or serum separation over a period of several
weeks could be attained by increasing the stabiliser content
to just 0.25 wt% (Cao, Dickinson, & Wedlock, 1991).
The inhibition of creaming at stabiliser concentrations
$0.125 wt% in Fig. 7 can be attributed to immobilisation
of the protein-coated oil droplets in a weak gel-like network
with a very high low-stress shear viscosity. Partial stabilisa-
tion at 0.0625 and 0.1 wt% xanthan can be mainly attributed
to slow movement of the ¯occulated droplets under gravity
due to the high viscosity of the continuous phase (Dickinson,
1993).
In an emulsion containing a mixture of hydrocolloid and
small-molecule surfactant, the nature of the hydrocolloid±
surfactant interactions can in¯uence both rheology and
Fig. 9. In¯uence of rhamsan gum on the creaming of small-molecule surfac-
tant-stabilised emulsions (30 wt% oil, 1 wt% surfactant, pH 7, ionic
strength 0.05 M) stored at 25 8C in 6 cm tubes. The time ts for the serum
layer to become visible to the unaided eye is plotted against the hydrocol-
loid concentration c: W, Tween 20; X, SDS. (Reproduced with permission
from Dickinson et al. (1993)).
stability. This is shown in Fig. 8 for two different emulsions
(30 wt% oil, 1 wt% surfactant) of similar average droplet
size (d43 < 0:6 mm), containing the same concentration
(0.1 wt%) of another anionic microbial polysaccharide,
rhamsan, but made with two different emulsi®ers: (i) non-
ionic Tween 20 and (ii) anionic sodium dodecyl sulfate
(SDS). Without emulsi®ed oil present, there was observed
no signi®cant difference in shear-thinning rheology of the
two mixed hydrocolloid 1 surfactant aqueous phases
(rhamsan 1 Tween or rhamsan 1 SDS); and neither emul-
sion showed any measurable change in mean droplet size on
storage for several days (Dickinson, Goller, & Wedlock,
1993). Fig. 8 shows that, for moderate applied stresses
(.1 Pa), the apparent viscosities of the two emulsions are
also similar, but at low stresses (,10 2 Pa) the Tween 20
emulsion viscosity is two orders of magnitude higher than
that of the SDS emulsion. This difference can be attributed
to the different effect of the charged polyelectrolyte on the
electrostatically stabilised SDS-coated emulsion droplets as
compared with its effect on the sterically stabilised Tween-
coated droplets (Dickinson et al., 1993).
There is often found to be a correlation between emulsion
rheology and emulsion creaming stability. For example, for
the same sets of emulsion systems containing rhamsan and
Tween 20 or SDS, Fig. 9 shows the creaming stability as a
function of rhamsan concentration (Dickinson et al., 1993).
The serum separation time ts is de®ned as the time when a
distinct serum layer becomes ®rst visible to the naked eye.
According to this criterion, whereas the 1% SDS system
becomes unstable to creaming in just one day, the equiva-
lent Tween system is stable for several days. Comparison of
Figs. 8 and 9 shows that the higher low-stress viscosity of
the Tween 20 emulsion correlates well with its better cream-
ing stability. The stronger gel-like network of the concen-
trated Tween-stabilised emulsion (30% oil), as measured by
the much higher h value at low S in Fig. 8, can more effec-
tively retard the thermodynamic drive towards depletion-
based phase separation. It is interesting to contrast this
case with the one shown in Fig. 6, where the enhanced
low-stress viscosity from bridging ¯occulation arises as a
result of an associative interaction between hydrocolloid
(pectin) and adsorbed protein (as1-casein). In the bridging
¯occulation case, the higher low-stress viscosity in the
concentrated emulsion (40% oil) correlates with poorer
creaming stability (i.e. a faster rate of serum separation) in
the diluted emulsion (Dickinson et al., 1998). This opposite
behaviour to that given in Fig. 9 for depletion ¯occulation
shows the complexity of interpreting stability/rheology rela-
tionships in hydrocolloid-containing emulsion systems.
Finally, it seems worthwhile to stress that ¯occulation
is a ubiquitous phenomenon in hydrocolloid-containing
systems. As illustrated by Lips et al. (1991) for a dilute
model colloid of polystyrene latex particles, a biopolymer
will tend either to cause ¯occulation by bridging (at about
half saturation coverage) or by depletion (at rather higher
concentrations). Which mechanism actually occurs in any
 E. Dickinson / Food Hydrocolloids 17 (2003) 25±39
particular system depends sensitively on the nature of the
hydrocolloid-particle interaction, which in turn is dependent
on the particle surface properties and the solution condi-
tions. In emulsions, the most likely situations favouring
destabilisation by ¯occulation (bridging or depletion) are
those where the oil volume fraction is low (say, 5±10%)
and where the aqueous phase contains a non-gelling hydro-
colloid (or a gelling hydrocolloid at a concentration below
the gelation threshold). In practice, of course, biopolymer
adsorption and ¯occulation effects in concentrated emul-
sions are commonly masked by the very high low-stress
viscosity of the hydrocolloid-containing aqueous phase or
by hydrocolloid gelation between the droplets.
6. Concluding remarks
Some food hydrocolloids are suf®ciently surface-active in
their own right to act as sole emulsifying agents during the
formation of oil-in-water emulsions. In most cases, it
appears that the origin of the emulsifying ability is the
presence of proteinaceous material covalently bound or
physically associated with the carbohydrate polymer. Typi-
cally, the emulsions produced are coarser than those that can
be made with low-molecular-weight water-soluble surfac-
tants or milk proteins at the same emulsi®er/oil ratio. Once
strongly adsorbed at the oil±water interface, however,
hydrocolloids can be even more effective than surfactants
or proteins in conferring long-term stability on emulsions.
This is due to the very favourable attributes of hydrophili-
city and large molecular size in connection with the ef®-
ciency of steric stabilisation. Hydrocolloids are especially
useful in practice for stabilisation of emulsions under the
acidic conditions where milk proteins are much less effective.
Hydrocolloids have an important role, both positive and
negative, in relation to the storage stability of food emul-
sions. Of course, this may simply be by modi®cation of the
small-deformation rheology of the continuous aqueous
phase. But, commonly also, the hydrocolloid in¯uences
the state of ¯occulation of the droplets via either a bridging
or depletion mechanism, depending on whether the hydro-
colloid has a net attractive or repulsive interaction with the
surface. As the latter typically consists of adsorbed protein,
an understanding of the factors affecting protein±polysac-
charide interactions in solution seems extremely valuable
for understanding and controlling the physico-chemical
phenomena involved. Even small changes in weak attractive
or repulsive interactions between different biopolymers in a
colloidal system can have a profound effect on physical
stability with respect to creaming, sedimentation or serum
separationÐwith drastic consequences for product quality
and appearance.
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