Food Hydrocolloids 19 (2005) 485491

www.elsevier.com/locate/foodhyd

Competitive adsorption of proteins with methylcellulose

and hydroxypropyl methylcellulose
Juan-Carlos Arboleya1, Peter J. Wilde*
Institute of Food Research, Norwich Research Park, Colney Lane, Norwich NR4 7UA, UK

Abstract
Surface-active polysaccharides are attracting increasing interest for use in a variety of applications. Amongst these, methylcellulose (MC)
and hydroxypropyl methylcellulose (HPMC) have been developed, in part, for their foam and emulsion stabilising properties, together with
their water holding and viscosity enhancing properties. The aim of this research is to quantify the competitive adsorption between proteins
and MC/HPMC, as they are often used together in many applications, and the results of potential effects of competition are unknown.
Two proteins were compared; b-lactoglobulin (BLG) and b-casein (BCAS). BLG forms an elastic interface, whereas BCAS does not.
Hence, BCAS is displaced by surfactants more easily than BLG. The surface rheology, surface tension and foam stability of the mixed
protein:polysaccharide systems were determined to elucidate the mechanism and consequences of competition.
In contrast to surfactants, both MC and HPMC formed highly elastic interfaces, more elastic even than BLG. Both HPMC and MC were
more surface active than the proteins, therefore at higher MC and HPMC concentrations, the polysaccharides began to dominate the
interfacial properties. Whereas surfactants reduce the elasticity of the protein adsorbed layer, the elastic properties of the polysaccharides
enhanced the overall strength of the interface, which will potentially result in more stable foams.
q 2005 Elsevier Ltd. All rights reserved.
Keywords: Methylcellulose; Hydroxypropyl methylcellulose; b-Lactoglobulin; b-Casein; Interface

1. Introduction
The formation and stability of foams and emulsions is a key
quality parameter in a wide range of applications. Particularly
in food since consumer perception of quality is strongly
influenced by appearance. Foam and emulsion functionality is
strongly influenced by the surface and interfacial properties of
the surface-active components in the system (Dickinson,
2001). Therefore, the role that these ingredients play is vital for
the formation and stability of food foams and emulsions. In
addition, the competition between the different surface-active
species can also be important for the functionality offoams and
emulsions. Competitive adsorption phenomena between
proteins and surfactants have been found to have a major
impact on foam and emulsion stability (Coke, Wilde, Russell,
& Clark, 1990; Dickinson, Owusu, & Williams, 1993).
* Corresponding author. Tel.: C44 1603 255258; fax: C44 1603 507723.
E-mail address: peter.wilde@bbsrc.ac.uk (P.J. Wilde).
1
Current address: AZTI (Instituto Tecnologico Pesquero y Alimentario)
Txatxarramendi Ugartea, z/g, 48395 Sukarrieta/Bizkaia, Spain.
0268-005X/$ - see front matter q 2005 Elsevier Ltd. All rights reserved.
doi:10.1016/j.foodhyd.2004.10.013

Therefore, this competitive adsorption behaviour has been

studied extensively over recent years (Bos & van Vliet, 2001;
Cornec et al., 1996; Cornec et al., 1998; Euston et al., 1996).
The importance is derived from the fact that proteins and
surfactants stabilise interfaces by very different mechanisms
(Wilde, Mackie, Husband, Gunning, & Morris, 2004).
Proteins form a visco-elastic adsorbed layer, which creates a
mechanical barrier against coalescence. In contrast, the fluid
layer formed by surfactants allows them to rapidly spread in
response to surface tension gradients. Both of these mechanisms rely on very different molecular properties and
interactions, and are therefore mutually incompatible, resulting in instability.
More recently, surface-active polysaccharides are
attracting increasing interest. Amongst these, methylcellulose (MC) and hydroxypropyl methylcellulose (HPMC)
have been developed, in part, for their foam and emulsion
stabilising properties (Dickinson, 2003; Dickinson & Izgi,
1996), together with their water holding (Sarkar & Walker,
1995) and viscosity enhancing properties (Wollenweber,
Makievski, Miller, & Daniels, 2000). Although their main

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J.-C. Arboleya, P.J. Wilde / Food Hydrocolloids 19 (2005) 485491

application in food emulsions is as a stabiliser or thickener

(Whistler, 1973), both MC and HPMC have demonstrated
significant surface activity (Sarkar, 1984). The properties of
the interfacial layers, especially the ratio of train/loop and
tail segments, and the elasticity of the layer, determine the
emulsion stability (Daniels & Barta, 1994), particularly the
coalescence stability of the oil droplets (Cardenasvalera &
Bailey, 1995). Hydrocolloids have been effective in
increasing the stability of foams through enhanced viscosity
that retards drainage (Stanley, Goff, & Smith 1996). The
foam activity of MC has also been shown to improve the
whippability of cake batters through partial replacement of
the egg white. The foam stability was further improved by
the gelation of the MC after heating (Grover, 1984). The
emulsion stabilizing properties of these compounds could
be associated with their structural features. Nahringbauer
(1995) has suggested that adsorption of hydrocolloids
includes two consecutive or simultaneous stages: a slow
diffusion of the macromolecules from the bulk phase to the
subsurface region followed by adsorption of polymer
segments to the interface. Also, it was proposed that,
similarly to proteins, adsorption was followed by changes in
molecular conformation. Initially, in bulk solution, the
macromolecules are coiled, but after adsorption the polymer
backbone starts to unfold. A model was proposed involving
unfolding or spreading of the adsorbed molecules followed
by attachment of the polymer segments from the subsurface
to the surface. This leads to an increase in the number of
adsorbed polymer segments causing a reduction of the
surface tension.
Proteinpolysaccharide interactions are very important
for a wide variety of applications (Benichou, Aserin, &
Garti, 2002; Kato, 2002) including the formation, structure
and physical properties of mixed gel systems (Turgeon,
Beaulieu, Schmitt, & Sanchez, 2003). However, the number
of studies on the foam and emulsion stabilising properties of
protein polysaccharide mixtures has been limited, despite
the functionality of certain gums, which rely on protein
polysaccharide interactions for their functionality (Benichou at al., 2002; Dickinson, 2003). Some studies have been
performed studying adsorption at solid surfaces (Fujimoto,
Reis, Petri, & Campana, 2002; Sierakowski, Freitas,
Fujimoto, & Petri, 2002), and looking at controlled multilayer formation for stabilising emulsions (Moreau, Kim,
Decker, & McClements, 2003). However, the competitive
adsorption of independent surface-active proteins and
polysaccharides has rarely been studied. Therefore, the
aim of this research is to quantify the effects of competitive
adsorption between proteins and MC/HPMC.

molecular weight 42 kDa methyl substitution between 27.0

and 30%; hydroxypropyl substitution between 3.0 and 5.5%)
were obtained from The Dow Chemical Company (Midland,
TX). b-Casein (BCAS; C-6905 minimum 90% by electrophoresis), and b-lactoglobulin (BLG; L-2506 approximately
80% purity), both derived from bovine milk, were purchased
from Sigma chemicals (Gillingham, UK). Measurements on
the mixed proteinpolysaccharide solutions were performed
at a fixed protein concentration of 10 mM (equivalent to
0.018 wt% BLG and 0.024 wt% BCAS) and variable MC
and HPMC concentrations (00.75 wt%). The protein
concentrations were chosen, as they were functionally
relevant in a separate study. The polysaccharide concentration range was chosen as it was commercially relevant,
and resulted in the whole range of interfacial behaviours
from protein dominated, through to polysaccharide dominated. All measurements were performed in 10 mM
phosphate buffer at pH 7.0. Polysaccharide solutions were
gently dispersed using a bench top magnetic stirrer for 1 h
then stored at 5 8C for different periods prior to measurement.

3. Methods
3.1. Surface tension
Surface tensions at the airwater interface of solutions of
protein and polysaccharides were measured using the
pendant drop technique. In this technique, surface/interfacial
tension was calculated from the size and shape of a drop
hanging from the tip of a syringe. The mathematical
treatment of pendant drop shape is based on the fundamental
equation of capillarity, which relates the interfacial/surface
tension to the pressure difference across a surface and to the
two principal radii of curvature of the surface at that point
(Ambwani & Fort, 1979). Droplets of the aqueous phase were
held by the tip of a syringe (diameter, 0.7 mm). The image
was digitised with a Pulnix TM500 monochrome camera
(resolution, 512!512 pixels) using a MuTech MV200 frame
grabber and a personal computer. The shape of the drop was
analysed by computer image analysis (Hansen & Rodsrud,
1991). Surface tension was also determined by the Wilhelmy
plate method. This apparatus consisted of a home-constructed tensiometer, which was made by a 10 g force
transducer (HBM, GmbH, Darmstadt, Germany) and a
25 mm wide roughened glass plate. The measuring system
was calibrated with a known weight before any contact
between plate and sample surface. Accuracy was estimated at
better than 0.1 mN/m. Surface tension was monitored at
room temperature for between 10 and 20 min, according to
the adsorption rate of each solution.

2. Materials
3.2. Surface rheology
Methyl cellulose (Methocel Premium A15, mean molecular weight 14 kDa, methyl substitution between 27.5
and 31.5%) and HPMC (Methocel HPM 450, mean

Surface shear rheological measurements were carried out

to study the mechanical and flow properties of adsorbed

J.-C. Arboleya, P.J. Wilde / Food Hydrocolloids 19 (2005) 485491

layers at fluid interfaces (Murray & Dickinson, 1996), and

are sensitive to surface structure and composition (Ridout,
Mackie, & Wilde, 2004). Experiments at the airwater
interface were made using a Bohlin CS10 controlled stress
rheometer using a 7 cm diameter bicone as measuring
geometry. The surface rheological response was tested by
oscillation mode at a frequency and stress of 0.5 Hz and
1.5!10K4 mN/m, respectively. Measurements were performed at room temperature.

487

Fig. 1 shows the results of preliminary surface rheological experiments designed to check for adverse storage or
temperature effects on the surface properties of 0.1% MC
and HPMC solutions. Fig. 1a shows the surface shear elastic
modulus (G 0 ) after 30 min adsorption time, following

storage of the MC/HPMC solutions for different times. In

general, there was a dramatic effect of storage time, showing
a large increase in G 0 over the first 35 days, followed by a
period of stability. Finally after 10 days storage, G 0 began to
decrease. MC initially formed a weaker interface, but during
the stable period it was stronger (G 0 z210 mN/m) compared
to HPMC (G 0 z130 mN/m). Subsequent experiments used
MC and HPMC solutions which had been stored for periods
which resulted in stable values of G 0 (310 days storage).
The reasons for the dramatic changes with storage time are
not clear, it is possible that changes in the state of hydration
of the MC or HPMC may affect molecular structure, and it
has been found that changes in hydration can occur for
periods of up to 4 days (McCrystal, Ford, & RajabiSiahboomi, 1997).
Fig. 1b shows that the surface rheology did show some
changes as a function of temperature, although, around
room temperature, the changes were within experimental
error at approximately 210G20 mN/m. At 10 8C, samples
showed weaker surfaces at 140G25 mN/m. Higher temperatures provoked a dramatic change in their rheological
properties, particularly above 50 8C (Kobayashi, Huang, &
Lodge, 1999). All future experiments were based on the
stable intervals of storage stability and experiments were
performed at 20 8C.
The surface tension of the individual components as a
function of concentration is shown in Fig. 2. All the
components seem to reach an initial saturation point around
0.001 wt%. However, the surface tension of the proteins
continued to decrease at higher concentrations. This is in
agreement with literature values (Wustneck et al., 1996).
The MC and HPMC are distinguishable from the proteins
in that they appear to be more surface active than the
proteins at all concentrations. The lowest values for the MC
and HPMC were between 46 and 48 mN/m, compared to

Fig. 1. Effect of storage time and temperature on the surface shear elasticity
of MC (B) and HPMC (:) after 30 min adsorption as a function of (a)
storage time and (b) temperature.

Fig. 2. Effect of concentration on the surface tension as measured by

the pendant drop technique for MC (B); HPMC (6); b-casein (%)
and b-lactoglobulin (&).

4. Results and discussion

4.1. Individual components

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J.-C. Arboleya, P.J. Wilde / Food Hydrocolloids 19 (2005) 485491

5052 mN/m for the proteins. It is interesting to note, that

for HPMC, above 0.02 wt%, the surface tension values
begin to increase slightly. This has been observed for some
surfactant systems where purity and molecular polydispersity can result in these types of effects around the cmc
(Fang & Joos, 1992).
Considering the surface behaviour of the individual
components, the mixtures of protein and polysaccharides
where then studied to evaluate the effects of competitive
adsorption.
4.2. Protein and MC
The surface properties of MCprotein mixtures were
determined. Fig. 3 shows the results of the surface tension
and surface rheological measurements of MC with BCAS
and BLG. The surface tension results (Fig. 3a) show that as
the MC concentration is increased, that the surface tension
of the protein solutions decreases, demonstrating that the
greater surface activity of the MC is affecting the surface
tension of the mixture. The values for the mixed systems
becomes very close to the MC alone around 0.1 wt% MC. In
the case of BCAS, above 0.1 wt% MC, all the values were

similar to MC alone, suggesting that MC was dominating

the surface properties above a concentration of 0.1 wt%. In
the other hand, BLGMC mixture showed a decrease of
surface tension from 52 to 46.5 mN/m up to 0.2%. From this
concentration, surface tension increased slightly up to
47 mN/m at 0.75% MC. This suggests that BLG is either
resisting displacement by MC, which has been found
previously (Mackie, Gunning, Wilde, & Morris, 1999). Or
that a complex between BLG and MC is resulting in a
surface with different characteristics to the pure components. To investigate this further, the surface rheological
properties of these mixtures was investigated.
The surface shear elastic modulus (G 0 ) of MCprotein
mixtures is shown in Fig. 3b. MC alone showed a high
surface elastic modulus value (O100 mN/m) at low
concentration and remained fairly constant above 0.3%
(w220 mN/m). BCAS alone forms a very weak adsorbed
layer (Dickinson, Rolfe, & Dalgleish, 1990) and seemed to
dominate the surface at low MC concentrations because of
the low values of elastic modulus. At higher MC
concentrations, BCAS was gradually replaced by MC
resulting in higher values of the surface elasticity (antagonistic effect). At 0.75% of MC, mixture showed similar
elastic behaviour to MC alone, which agrees with the
surface tension results and suggests more or less complete
displacement of BCAS molecules from the airwater
interface. Slightly different behaviour was found in the
presence of BLG (Fig. 3b). In this case, at low MC
concentrations, the mixture showed higher elastic modulus
values than BCAS mixtures and it reached MC values
between 0.1 and 0.2%. This behaviour from the mixture can
be expected due to the viscoelastic nature of the BLG
adsorbed layer. Both components seemed to work synergistically to enhance the elasticity of the interface. This is an
interesting result from the practical point of view for an
improvement of the functionality of BLG by adding small
amounts of MC. At higher MC concentrations, the mixture
recorded even greater elastic values than isolated MC,
which may suggest synergistic interactions between both
components.
4.3. HPMC and protein

Fig. 3. Effect of MC concentration on (a) surface tension and (b) surface

shear elasticity of solutions containing: no protein (!); or 10 mM b-casein
(6) or b-lactoglobulin (&).

The surface tension and rheological properties of

proteinHPMC mixtures a shown in Fig. 4. As suggested
earlier, the surface tension of HPMC alone recorded higher
surface tension values as the HPMC concentration was
increased. This unusual behaviour was confirmed by using
another technique. Wilhelmy plate results showed how
surface tension increased from 47.5 to 48.5 mN/m at a range
concentration from 0.01 to 0.1%. At 0.3%, surface tension
reached equilibrium at 53 mN/m up to 0.75% (Fig. 4a). It
has been reported (Fang & Joos, 1992) that experiments of
SDS showed an minimum in the surface tension close to the
cmc caused by impurities in the product. Therefore,
polydispersity in the molecular weight or degree of

J.-C. Arboleya, P.J. Wilde / Food Hydrocolloids 19 (2005) 485491

Fig. 4. Effect of HPMC concentration on (a) surface tension and (b) surface
shear elasticity of solutions containing: no protein (!, B); or 10 mM bcasein (6) or b-lactoglobulin (&). Open circles represent surface tensions
measured by the Wilhelmy plate technique for comparison.

substitution may result in this effect. HPMC with mixtures

of BCAS and BLG showed a decrease in surface tension at
low concentrations of HPMC with similar values to isolated
HPMC. However, from 0.01 to 0.05% for BLG and BCAS,
respectively, a dramatic increase occurred and reached
values around 54.4 and 53 mN/m for BLG and BCAS,
respectively, between 0.1 and 0.3%. From 0.3%, surface
tension of BLG mixture decreased to reach similar values to
HPMC alone, whereas BCAS mixture remained a constant
at 53 mN/m, similar to HPMC alone. This was most unusual
behaviour, even for mixtures, but it was consistent and
repeatable, and possible connected with the unusual surface
tension behaviour of HPMC alone over this concentration
range.
Surface shear rheological measurements were carried out
over the same HPMC concentration range, alone and in the
presence of BCAS and BLG at a constant concentration
(10 mM). Elastic modulus of HPMC alone showed lower
values compared to MC alone (Fig. 3b). At 0.1%, HPMC
already reached a maximum at around 130 mN/m and

489

remained high, but slightly lower values up to 0.75%. For

the BCASHPMC mixture, displacement of BCAS
appeared to occur at a low HPMC concentration (0.05%
HPMC) as G 0 reached a value similar to HPMC alone.
However, the surface became weaker again between 0.1 and
0.2% HPMC. This behaviour was highly reproducible.
Above that concentration HPMC seemed to control the
surface space because of the similar values of the isolated
compound and the mixture.
Similar behaviour was observed in BLGHPMC mixtures. G 0 values of the mixture exceeded isolated HPMC
values at lower HPMC concentrations and reached a
maximum at 190 mN/m with 0.1% HPMC. G 0 then
decreased to 50 mN/m at 0.3% HPMC and from that
concentration, HPMC started to dominate the surface. At
0.5% HPMC, elasticity showed similar behaviour to HPMC
alone. In addition, the higher elastic modulus compared to
BCASHPMC mixture supports the idea to have synergistic
behaviour in the presence of BLG.
When an adsorbed surfactant molecule orients itself at
the interface, there is a decrease of free energy resulting in a
lowering of surface tension (Dickinson & Stainsby, 1982).
Unfortunately, this simple model becomes extremely
complicated for polymers, where hydrophilic and hydrophobic regions are not well defined. They form threedimensional structures that make adsorption at the interface
a much more complex process (Dickinson, 2003; Norde,
MacRitchie, Nowicka, & Lyklema, 1986). In addition, the
higher molecular weight of HPMC compared to MC studied
here can make the diffusion to the interface slower and
therefore result in a higher surface tension. This molecule
can show a non-uniform configuration of hydrophilic and
hydrophobic blocks where the adsorption can be more
difficult (Sarkar, 1984). At different concentrations, the
different molecular configurations will be at different stages
in their adsorption isotherm and this may result in complex
adsorption behaviour. The main feature of this competitive
adsorption study is that the molecule competing with the
protein has a greater surface elasticity than the protein.
Conventional studies have involved small molecular weight
surfactants, which are generally mobile at the surface, and
therefore have negligible surface elasticity. This incompatibility in fact drives molecular segregation at the interface.
Whereas, in this case, with two competing polymers, that
both form immobile interfaces, the surface dynamics will be
completely different. In the case of MC, there appears to be
a fairly simple competition with the proteins for the
interface. The MC is more surface active than the proteins,
and eventually dominates the interfacial properties at higher
concentrations. This process is completed at lower MC
concentrations in the case of BCAS. This is probably
because BCAS forms a very weak surface, and is known to
be displaced at lower surface pressures (Mackie et al.,
1999), and lower concentrations (Cornec et al., 1998) than
BLG. In the case of BLG, the situation is a little more
complicated because we have two competing polymers,

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J.-C. Arboleya, P.J. Wilde / Food Hydrocolloids 19 (2005) 485491

both of which can form highly elastic surfaces. In addition,

BLG is able to bind with hydrophobic ligands (Coke et al.,
1990). The results suggest that instead of a simple
competitive displacement of the protein by MC, some
synergism occurs between the two adsorbed molecules, and
at relatively low concentrations of MC, resulting in higher
surface tensions and surface elasticities than either component. In fact G 0 for the mixed BLG:MC is higher than the
additive values of the individual components above 0.2 wt%
MC (Fig. 3b). It is unlikely that the packing density is
greater with the two components, as the surface tension of
the mixtures is actually higher. Therefore, it is more likely
that synergistic interactions, probably electrostatically
mediated, that lead to the synergistic increase in G 0 . This
has been observed with other protein:polysaccharide
systems (Sarker & Wilde, 1999; Sarker, Wilde, & Clark,
1998).
In the case of HPMC, similar behaviour between the two
proteins was observed. BCAS was affected by the increase
in HPMC concentration earlier than BLG, for the same
reasons as discussed above for MC. However, the situation
was complicated by the complex surface behaviour of
HPMC alone. Once the HPMC had reached its minimum
surface tension, around 0.01 wt%, the surface tension
increased slightly with increasing HPMC concentration.
This effect has been observed with the complex micelle
formation of SDS solutions when dodecanol is present
as an impurity (Fang & Joos, 1992), it has also been
observed in mixed surfactant systems (Wickham, Wilde, &
Fillery-Travis, 2002). Therefore, it is possible that the
polydisperse nature of the molecular weight and level of
substitution of the HPMC used in this study may result in
this surface tension effect. The unusual behaviour of the
surface elasticity of HPMC in the presence of protein, was
remarkably reproducible. The competition between competing, adsorbing species is initially based on surface activity
of the individual components, and controls the surface
competition (Ridout et al., 2004), and hence the
surface rheological properties. Therefore, the changing
surface activity of the HPMC as the concentration is
increased, is likely to strongly influence the competitive
adsorption with the added proteins. Hence, resulting in the
unusual behaviour of the mixtures. More specifically, as
the HPMC concentration increased above 0.1 wt%, the
surface tension of HPMC increased to levels above that of
BCAS alone, and then above BLG alone (Fig. 4a). This will
allow the proteins to adsorb in preference to the HPMC, and
hence the surface G 0 began to decrease towards values
associated with the protein alone. As the HPMC concentration increased further, the surface tension increased only
a little more, but the dynamics of adsorption would become
much quicker, and would therefore dominate the surface
behaviour before significant protein adsorption took place.
The surface rheology of the HPMC is great enough that
significant displacement of HPMC by the protein is unlikely
to occur (Mackie et al., 1999).

Another consideration is the interactions between the

proteins and polysaccharides in solution. This is another
area of widespread study, as it is known that interactions or
incompatibilities between proteins and polysaccharides
allow structures to develop in solution (Turgeon et al.,
2003). This may well influence the rate and extent of
adsorption. Consequentially, the order in which the different
components arrive at the interface will influence the final,
equilibrium surface composition (Damodaran & Rammovsky, 2003; Ridout et al., 2004). As a result of these
interactions in solution, the adsorption and hence the
functional properties of the system may well be affected.
The impact may be positive in terms of synergistic
interactions giving rise to increased surface elasticity, or
they may be negative as a result of hindered adsorption and
higher interfacial tensions. In any case, a thorough
investigation of the effects of these interactions is necessary
to understand the functionality of these complex mixtures.

5. Conclusion
The competitive adsorption of MC and hydroxypropylmethyl cellulose with two different proteins (BCAS and
BLG) was investigated. BCAS appeared to be displaced
through simple competitive adsorption, more easily than
BLG. Some synergism appeared to take place between the
adsorbed polysaccharides and BLG, resulting in greater
values of surface elasticity in the mixtures. Complex
adsorption behaviour of HPMC alone had a strong influence
on the competition with the proteins, resulting in complex,
non-linear concentration dependent behaviour. This underpinning knowledge of the complex surface behaviour of
these mixtures should allow the design of protein:polysaccharide mixtures with enhanced functionality.

Acknowledgements
The authors would like to thank Fraser Hogg, Dr Neil
Carr, and Dr Alan Holmes for their funding and support, and
to Dr Annette Fillery-Travis for her help and advice for this
project. PJW also acknowledges BBSRC for support
through the Core Strategic Grant to the Institute.

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