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Food Hydrocolloids 19 (2005) 485–491

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

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: (P.J. Wilde).
Current address: AZTI (Instituto Tecnolo´gico Pesquero y Alimentario)
Txatxarramendi Ugartea, z/g, 48395 Sukarrieta/Bizkaia, Spain.
0268-005X/$ - see front matter q 2005 Elsevier Ltd. All rights reserved.

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

especially the ratio of train/loop and tail segments. 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. 2002) including the formation. b-Casein (BCAS. L-2506 approximately 80% purity). The protein concentrations were chosen. The shape of the drop was analysed by computer image analysis (Hansen & Rodsrud. 2003). and looking at controlled multilayer formation for stabilising emulsions (Moreau. The mathematical treatment of pendant drop shape is based on the fundamental equation of capillarity. 1973). Kato. Surface rheology Methyl cellulose (Methocel Premium A15. but after adsorption the polymer backbone starts to unfold. Droplets of the aqueous phase were held by the tip of a syringe (diameter. Freitas. Dickinson.0. 1995). Reis. structure and physical properties of mixed gel systems (Turgeon. the aim of this research is to quantify the effects of competitive adsorption between proteins and MC/HPMC. & Smith 1996). the macromolecules are coiled. similarly to proteins. 2002). Decker. & Sanchez.J. mean molecular weight 14 kDa. Darmstadt.024 wt% BCAS) and variable MC and HPMC concentrations (0–0. 2003). molecular weight 42 kDa methyl substitution between 27. according to the adsorption rate of each solution. and the elasticity of the layer. Initially. which was made by a 10 g force transducer (HBM. 2003). The foam activity of MC has also been shown to improve the whippability of cake batters through partial replacement of the egg white. 512!512 pixels) using a MuTech MV200 frame grabber and a personal computer. Protein–polysaccharide interactions are very important for a wide variety of applications (Benichou. Materials 3. The emulsion stabilizing properties of these compounds could be associated with their structural features. The polysaccharide concentration range was chosen as it was commercially relevant. through to polysaccharide dominated.75 wt%). Aserin. The foam stability was further improved by the gelation of the MC after heating (Grover. Methods 3. surface/interfacial tension was calculated from the size and shape of a drop hanging from the tip of a syringe. Schmitt. Kim. Wilde / Food Hydrocolloids 19 (2005) 485–491 application in food emulsions is as a stabiliser or thickener (Whistler.5%) were obtained from The Dow Chemical Company (Midland. both MC and HPMC have demonstrated significant surface activity (Sarkar.5 and 31. in bulk solution. Petri.0 and 30%.5%) and HPMC (Methocel HPM 450. Surface tension was also determined by the Wilhelmy plate method. The measuring system was calibrated with a known weight before any contact between plate and sample surface. 1984). despite the functionality of certain gums. TX). Surface tension was monitored at room temperature for between 10 and 20 min. and b-lactoglobulin (BLG. 1979). 1991). which rely on protein polysaccharide interactions for their functionality (Benichou at al. & McClements. 2002. Goff. methyl substitution between 27. Sierakowski. the number of studies on the foam and emulsion stabilising properties of protein polysaccharide mixtures has been limited. hydroxypropyl substitution between 3. The properties of the interfacial layers. However.0 and 5.1. 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. particularly the coalescence stability of the oil droplets (Cardenasvalera & Bailey. & Petri.018 wt% BLG and 0. 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. mean Surface shear rheological measurements were carried out to study the mechanical and flow properties of adsorbed . Accuracy was estimated at better than 0. 1984). Some studies have been performed studying adsorption at solid surfaces (Fujimoto. both derived from bovine milk. In this technique. Hydrocolloids have been effective in increasing the stability of foams through enhanced viscosity that retards drainage (Stanley. were purchased from Sigma chemicals (Gillingham. 3. & Garti. 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.1 mN/m. determine the emulsion stability (Daniels & Barta. P. and resulted in the whole range of interfacial behaviours from protein dominated.. GmbH.486 J. All measurements were performed in 10 mM phosphate buffer at pH 7. However. 2. Beaulieu. as they were functionally relevant in a separate study.2. Germany) and a 25 mm wide roughened glass plate. The image was digitised with a Pulnix TM500 monochrome camera (resolution. Therefore. adsorption was followed by changes in molecular conformation. C-6905 minimum 90% by electrophoresis). 0. Arboleya. 2002. Surface tension Surface tensions at the air–water interface of solutions of protein and polysaccharides were measured using the pendant drop technique. This apparatus consisted of a home-constructed tensiometer. & Campana. the competitive adsorption of independent surface-active proteins and polysaccharides has rarely been studied.-C. UK). Measurements on the mixed protein–polysaccharide solutions were performed at a fixed protein concentration of 10 mM (equivalent to 0. 1994). 2002. Also. Fujimoto. it was proposed that.7 mm).

Fig.5 Hz and 1. Wilde / Food Hydrocolloids 19 (2005) 485–491 layers at fluid interfaces (Murray & Dickinson. 2004). the surface tension of the proteins continued to decrease at higher concentrations. Fig. & Lodge. HPMC (6). & RajabiSiahboomi. At 10 8C. the changes were within experimental error at approximately 210G20 mN/m.J.001 wt%. All future experiments were based on the stable intervals of storage stability and experiments were performed at 20 8C. b-casein (%) and b-lactoglobulin (&). The surface rheological response was tested by oscillation mode at a frequency and stress of 0. The surface tension of the individual components as a function of concentration is shown in Fig. Higher temperatures provoked a dramatic change in their rheological properties. Huang. All the components seem to reach an initial saturation point around 0. 4. MC initially formed a weaker interface. Effect of concentration on the surface tension as measured by the pendant drop technique for MC (B). but during the stable period it was stronger (G 0 z210 mN/m) compared to HPMC (G 0 z130 mN/m). particularly above 50 8C (Kobayashi. Finally after 10 days storage.-C. P. & Wilde. The MC and HPMC are distinguishable from the proteins in that they appear to be more surface active than the proteins at all concentrations. Individual components . 2. and it has been found that changes in hydration can occur for periods of up to 4 days (McCrystal. 2. although. 1997).5!10K4 mN/m.. However. 1 shows the results of preliminary surface rheological experiments designed to check for adverse storage or temperature effects on the surface properties of 0. followed by a period of stability. 1b shows that the surface rheology did show some changes as a function of temperature. Mackie. Subsequent experiments used MC and HPMC solutions which had been stored for periods which resulted in stable values of G 0 (3–10 days storage). there was a dramatic effect of storage time. and are sensitive to surface structure and composition (Ridout. following storage of the MC/HPMC solutions for different times.1. compared to Fig. Ford. 1996). Fig. The reasons for the dramatic changes with storage time are not clear. This is in agreement with literature values (Wustneck et al. 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. 1. samples showed weaker surfaces at 140G25 mN/m. it is possible that changes in the state of hydration of the MC or HPMC may affect molecular structure. 1996). 487 Fig.1% MC and HPMC solutions.J. Experiments at the air–water interface were made using a Bohlin CS10 controlled stress rheometer using a 7 cm diameter bicone as measuring geometry. G 0 began to decrease. The lowest values for the MC and HPMC were between 46 and 48 mN/m. Arboleya. Measurements were performed at room temperature. In general. 1a shows the surface shear elastic modulus (G 0 ) after 30 min adsorption time. showing a large increase in G 0 over the first 3–5 days. 1999). respectively. around room temperature. Results and discussion 4.

3. surface tension increased slightly up to 47 mN/m at 0.3% (w220 mN/m).5 to 48. BLG–MC mixture showed a decrease of surface tension from 52 to 46.1 wt% MC. the surface rheological properties of these mixtures was investigated. 4. 3 shows the results of the surface tension and surface rheological measurements of MC with BCAS and BLG.2%. 4. that the surface tension of the protein solutions decreases. At 0. which has been found previously (Mackie.5 mN/m at a range concentration from 0. In the case of BCAS.75% MC. Arboleya. The values for the mixed systems becomes very close to the MC alone around 0. 4. polydispersity in the molecular weight or degree of .75% of MC. Considering the surface behaviour of the individual components. From this concentration. In the other hand. & Morris. To investigate this further. or 10 mM b-casein (6) or b-lactoglobulin (&). At higher MC concentrations. The surface tension results (Fig.-C. It is interesting to note.3. At higher MC concentrations. It has been reported (Fang & Joos. BCAS alone forms a very weak adsorbed layer (Dickinson. 3b. 3a) show that as the MC concentration is increased. Or that a complex between BLG and MC is resulting in a surface with different characteristics to the pure components.01 to 0.1 wt%. all the values were similar to MC alone. above 0. Slightly different behaviour was found in the presence of BLG (Fig. the surface tension of HPMC alone recorded higher surface tension values as the HPMC concentration was increased. 1992).02 wt%. at low MC concentrations.5 mN/m up to 0. Wilde / Food Hydrocolloids 19 (2005) 485–491 50–52 mN/m for the proteins. above 0. This suggests that BLG is either resisting displacement by MC. surface tension reached equilibrium at 53 mN/m up to 0. Protein and MC The surface properties of MC–protein mixtures were determined. Both components seemed to work synergistically to enhance the elasticity of the interface. Effect of MC concentration on (a) surface tension and (b) surface shear elasticity of solutions containing: no protein (!). The surface tension and rheological properties of protein–HPMC mixtures a shown in Fig. In this case. the mixture recorded even greater elastic values than isolated MC.1 and 0. mixture showed similar elastic behaviour to MC alone. As suggested earlier. the mixture showed higher elastic modulus values than BCAS mixtures and it reached MC values between 0. which may suggest synergistic interactions between both components. This unusual behaviour was confirmed by using another technique. demonstrating that the greater surface activity of the MC is affecting the surface tension of the mixture. 3b). Gunning. The surface shear elastic modulus (G 0 ) of MC–protein mixtures is shown in Fig.1 wt% MC. 4a).75% (Fig. which agrees with the surface tension results and suggests more or less complete displacement of BCAS molecules from the air–water interface. Therefore. the mixtures of protein and polysaccharides where then studied to evaluate the effects of competitive adsorption. Rolfe. the surface tension values begin to increase slightly. BCAS was gradually replaced by MC resulting in higher values of the surface elasticity (antagonistic effect). Wilhelmy plate results showed how surface tension increased from 47. & Dalgleish. HPMC and protein Fig. P.2%. 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.2. 1992) that experiments of SDS showed an minimum in the surface tension close to the cmc caused by impurities in the product. Fig. MC alone showed a high surface elastic modulus value (O100 mN/m) at low concentration and remained fairly constant above 0. suggesting that MC was dominating the surface properties above a concentration of 0. 1990) and seemed to dominate the surface at low MC concentrations because of the low values of elastic modulus.3%.1%. Wilde.J.488 J. that for HPMC. This behaviour from the mixture can be expected due to the viscoelastic nature of the BLG adsorbed layer. At 0. 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. 1999).

2% HPMC. but it was consistent and repeatable. In the case of MC. and is known to be displaced at lower surface pressures (Mackie et al. In the case of BLG. 4. When an adsorbed surfactant molecule orients itself at the interface.05% for BLG and BCAS.05% HPMC) as G 0 reached a value similar to HPMC alone. At different concentrations. the surface became weaker again between 0.1% HPMC. the surface dynamics will be completely different. 1986). Wilde / Food Hydrocolloids 19 (2005) 485–491 Fig. 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. which are generally mobile at the surface.01 to 0. At 0.3%. in this case. Unfortunately. the situation is a little more complicated because we have two competing polymers. Norde.. 2003..5% HPMC. surface tension of BLG mixture decreased to reach similar values to HPMC alone.3%.1 and 0.1%. even for mixtures. This molecule can show a non-uniform configuration of hydrophilic and hydrophobic blocks where the adsorption can be more difficult (Sarkar. HPMC started to dominate the surface. with two competing polymers. This was most unusual behaviour. and possible connected with the unusual surface tension behaviour of HPMC alone over this concentration range. the different molecular configurations will be at different stages in their adsorption isotherm and this may result in complex adsorption behaviour. there appears to be a fairly simple competition with the proteins for the interface. and therefore have negligible surface elasticity. similar to HPMC alone. This behaviour was highly reproducible. G 0 values of the mixture exceeded isolated HPMC values at lower HPMC concentrations and reached a maximum at 190 mN/m with 0. whereas BCAS mixture remained a constant at 53 mN/m. HPMC with mixtures of BCAS and BLG showed a decrease in surface tension at low concentrations of HPMC with similar values to isolated HPMC. respectively. This incompatibility in fact drives molecular segregation at the interface. Conventional studies have involved small molecular weight surfactants.-C. Arboleya. this simple model becomes extremely complicated for polymers. Whereas.J. 1999). However. or 10 mM bcasein (6) or b-lactoglobulin (&). B). At 0. between 0. but slightly lower values up to 0. 1998) than BLG. Nowicka. They form threedimensional structures that make adsorption at the interface a much more complex process (Dickinson. HPMC already reached a maximum at around 130 mN/m and 489 remained high. G 0 then decreased to 50 mN/m at 0. the higher elastic modulus compared to BCAS–HPMC mixture supports the idea to have synergistic behaviour in the presence of BLG. Open circles represent surface tensions measured by the Wilhelmy plate technique for comparison. Surface shear rheological measurements were carried out over the same HPMC concentration range.3% HPMC and from that concentration. 1982). In addition. . However.1 and 0. and lower concentrations (Cornec et al. displacement of BCAS appeared to occur at a low HPMC concentration (0.J. & Lyklema. a dramatic increase occurred and reached values around 54. and eventually dominates the interfacial properties at higher concentrations. Effect of HPMC concentration on (a) surface tension and (b) surface shear elasticity of solutions containing: no protein (!. Above that concentration HPMC seemed to control the surface space because of the similar values of the isolated compound and the mixture. This process is completed at lower MC concentrations in the case of BCAS. there is a decrease of free energy resulting in a lowering of surface tension (Dickinson & Stainsby. The MC is more surface active than the proteins. elasticity showed similar behaviour to HPMC alone.75%. The main feature of this competitive adsorption study is that the molecule competing with the protein has a greater surface elasticity than the protein. MacRitchie. Similar behaviour was observed in BLG–HPMC mixtures. This is probably because BCAS forms a very weak surface. where hydrophilic and hydrophobic regions are not well defined. From 0. In addition. that both form immobile interfaces. 3b). from 0. Elastic modulus of HPMC alone showed lower values compared to MC alone (Fig. substitution may result in this effect. P. alone and in the presence of BCAS and BLG at a constant concentration (10 mM). For the BCAS–HPMC mixture. 1984).4 and 53 mN/m for BLG and BCAS. respectively.

equilibrium surface composition (Damodaran & Rammovsky. 2003). as the HPMC concentration increased above 0. A. This will allow the proteins to adsorb in preference to the HPMC. In fact G 0 for the mixed BLG:MC is higher than the additive values of the individual components above 0.1 wt%.. Hence. that lead to the synergistic increase in G 0 . 5. This effect has been observed with the complex micelle formation of SDS solutions when dodecanol is present as an impurity (Fang & Joos. was remarkably reproducible. S. adsorbing species is initially based on surface activity of the individual components. resulting in higher surface tensions and surface elasticities than either component. resulting in complex. and hence the surface G 0 began to decrease towards values associated with the protein alone. (2002). Wilde / Food Hydrocolloids 19 (2005) 485–491 both of which can form highly elastic surfaces. J. similar behaviour between the two proteins was observed. Advances in Colloid and Interface Science. Journal of Dispersion Science and Technology. As a result of these interactions in solution. Good. 1992). Interfacial rheological properties of adsorbed protein layers and surfactants: a review. More specifically. 1999. This has been observed with other protein:polysaccharide systems (Sarker & Wilde. and to Dr Annette Fillery-Travis for her help and advice for this project. and would therefore dominate the surface behaviour before significant protein adsorption took place. Sarker. & Clark. T. PJW also acknowledges BBSRC for support through the Core Strategic Grant to the Institute.01 wt%. BCAS was affected by the increase in HPMC concentration earlier than BLG. the changing surface activity of the HPMC as the concentration is increased. Surface and colloid science (pp. BLG is able to bind with hydrophobic ligands (Coke et al.2 wt% MC (Fig. the situation was complicated by the complex surface behaviour of HPMC alone. and controls the surface competition (Ridout et al. and Dr Alan Holmes for their funding and support. as the surface tension of the mixtures is actually higher. M... a thorough investigation of the effects of these interactions is necessary to understand the functionality of these complex mixtures. References Ambwani. A. Bos. 93–123. but the dynamics of adsorption would become much quicker. 1999). 91(3). Another consideration is the interactions between the proteins and polysaccharides in solution.. This underpinning knowledge of the complex surface behaviour of these mixtures should allow the design of protein:polysaccharide mixtures with enhanced functionality. Therefore. 2003. D. (2001). As the HPMC concentration increased further. some synergism occurs between the two adsorbed molecules.. In R. Benichou. or they may be negative as a result of hindered adsorption and higher interfacial tensions. This may well influence the rate and extent of adsorption..490 J. Stromberg (Eds. Arboleya. Aserin. Acknowledgements The authors would like to thank Fraser Hogg. and hence the surface rheological properties. Some synergism appeared to take place between the adsorbed polysaccharides and BLG. . Conclusion The competitive adsorption of MC and hydroxypropylmethyl cellulose with two different proteins (BCAS and BLG) was investigated. Wilde. 2004). as it is known that interactions or incompatibilities between proteins and polysaccharides allow structures to develop in solution (Turgeon et al.J. 3b). the surface tension increased slightly with increasing HPMC concentration. the order in which the different components arrive at the interface will influence the final. the surface tension of HPMC increased to levels above that of BCAS alone. Ridout et al.. resulting in the unusual behaviour of the mixtures. 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 surface rheology of the HPMC is great enough that significant displacement of HPMC by the protein is unlikely to occur (Mackie et al. is likely to strongly influence the competitive adsorption with the added proteins. more easily than BLG. Protein–polysaccharide interactions for stabilization of food emulsions. BCAS appeared to be displaced through simple competitive adsorption. Pendant drop technique for measuring liquid boundary tensions. & Garti.. Once the HPMC had reached its minimum surface tension. it is more likely that synergistic interactions. The results suggest that instead of a simple competitive displacement of the protein by MC. 1990). the surface tension increased only a little more. and at relatively low concentrations of MC. P. In any case. it has also been observed in mixed surfactant systems (Wickham. N. The unusual behaviour of the surface elasticity of HPMC in the presence of protein. A. 23(1–3).-C. It is unlikely that the packing density is greater with the two components. for the same reasons as discussed above for MC. (1979). In the case of HPMC.. & R. 2004). 4a). Consequentially. Wilde. probably electrostatically mediated. & Fort. non-linear concentration dependent behaviour. the adsorption and hence the functional properties of the system may well be affected. & van Vliet. around 0. The impact may be positive in terms of synergistic interactions giving rise to increased surface elasticity. The competition between competing.). 1998). and then above BLG alone (Fig. 93–119). In addition. New York: Plenum Press. This is another area of widespread study. However. resulting in greater values of surface elasticity in the mixtures. T. 2002). Complex adsorption behaviour of HPMC alone had a strong influence on the competition with the proteins. 437–471. R. & Fillery-Travis. Dr Neil Carr. Therefore.

. Structural interpretation of the interfacial properties of aqueous-solutions of methylcellulose and hydroxypropyl methylcellulose. A.. Colloids in food. 2(2). 61(5).. & Campana. Food hydrocolloids—3 (p. A.. & Joos. E. E. (1996). I. 25–39. R. A. E. Huang. S.. Advances in Colloid and Interface Science. & Sanchez. & Morris. F. Food Science and Technology International. A. M. F. D. (1998). Makievski.. Cereal Chemistry.. Glicksman (Ed. Wollenweber. 29(1). A. 237–244. Cornec.. F. Sarkar. (2002). S. A study on the interaction of water and cellulose ethers using differential scanning calorimetry. A.J. 25(4). J. 97(1). 113(1-2). The submicellar systems. A. London and New York: Applied Science Publishers. Gunning. & Barta. . Journal of Colloid and Interface Science. (1973). (1996). 12. Journal of Food Science.. Russell. Gunning. R. A. Journal of the Chemical Society—Faraday Transactions. Husband. 189–194.. Coke. thermodynamic and structural aspects. & Petri. J. 75(4). Food Science and Technology Research. Mackie. Oil-inwater emulsions stabilized by sodium caseinate or whey protein isolate as influenced by glycerol monostearate.. Wilde. R. K. G.. Sarker. & Walker. Turgeon. W. (2003). 191–201. 1. & McClements. 27. (1991)... W. Food Hydrocolloids.. & Clark. P. D. Journal of Colloid and Interface Science. (1982). (2001). 52(12).-C. 294(1). (1999). 401–414. 1. 8(3). 355–363. E. 17(3). R. D. Colloids Surfaces A: Physicochemical and Engineering Aspects. Kragel. P. Wilde. J.. Miller.. C. Enhancement of protein foam stability by formation of wheat arabinoxylan–protein crosslinks. 65(2–3). Proteins and emulsifiers at liquid interfaces. K. P. Journal of Food Science. P. 7070–7077. R. 172(1–3). Hydrocolloids at interfaces and the influence on the properties of dispersed systems.. Graft-copolymers as stabilizers for oil-in-water emulsions. Cornec. P. (2002).. Moreau. & Lzgi. E. 141(1). 25(5). Whistler. (1984). Petri. 89(5). A. B. G. & Williams. Industrial applications of Maillard-type protein– polysaccharide conjugates. C. F. Journal of Agricultural and Food Chemistry. Interfacial properties. (1997). Food Hydrocolloids. Kim. C. Colloids and Surfaces B-Biointerfaces. C. Sarker. Nowicka. 91–101.. Journal of Colloid and Interface Science. Wilde. 112(2). 203–213. J. 176(2).. 128–133. K. L. Boca Raton. G. Orthokinetic destabilisation of a protein-stabilised emulsion by a water soluble surfactant.. Norde.. A.. (1986). S. M. A. & Dalgleish. Protein– polysaccharide interactions: Phase-ordering kinetics. E. E. & Bailey. (1996). Gunning. Wilde. A.. Wilde / Food Hydrocolloids 19 (2005) 485–491 Cardenasvalera. J.. Fainerman. V. 157–166.. D. 481–486. 113–120. C. I. P.. K. P. Wickham. 491 McCrystal. & Fillery-Travis. A. M. S. A. D. D. 63(1). 114(1). V. C. A. Sarkar. 138. J. 493–499. K. 108–109. R. J. Current Opinion in Colloid and Interface Science. J. Ford. Competitive adsorption and thermodynamic incompatibility of mixing of beta-casein and gum arabic at the air–water interface. Adsorption behavior of oxidized galactomannans onto amino-terminated surfaces and their interaction with bovine serum albumin. (1995). (1990). E. Biochimica et Biophysica Acta-Molecular and Cell Biology of Lipids. Dynamic surface-tension and adsorption properties of b-casein and b-lactoglobulin. Husband. Fujimoto. Ridout. (1999).. Daniels. Wilde. 916–920. V.. 131–145. Emulsion stability as affected by competitive adsorption between an oil-soluble emulsifier and milk proteins at the interface. Grover. Kobayashi. 395–405. K. 318–328. 40(3). & Clark. Foam stabilization by proteinpolysaccharide complexes. Euston. J.. Interfacial rheology and the dynamic properties of adsorbed films of food proteins and surfactants. Milk protein interfacial layers and the relationship to emulsion stability and rheology. 2. & Lyklema. 177–185. M. E. Ethyl(hydroxyethyl)cellulose (BERMOCOLL cst-103). Mackie. Singh. The orogenic displacement of protein from the air/water interface by surfactant. A. Dickinson. & Morris.. Goff. J.. C. R. 17(1). Thermochimica Acta. M. 10(4). D. The dynamic surface-tension of SDSdodecanol mixtures. R. Surface shear viscometry as a probe of protein–protein interactions in mixed milk protein films adsorbed at the oil water interface. 121). J. J. MacRitchie.. P.. A. (1996). Sierakowski. P. Freitas. Dickinson. Kato. P. Schmitt. S. 757–761. Journal of Colloid and Interface Science. Reis. D. & Stainsby. Industrial gums polysaccharides and their derivatives2nd ed (pp. A. Sarker. D. N. 489–504. Fujimoto.. R. (2003). Pharmacopeial cellulose ethers as oil-inwater emulsifiers. Decker. European Journal of Pharmaceutics and Biopharmaceutics. R. Mackie.. Adsorption of hydroxypropyl methylcellulose at the liquid/liquid interface and the effect on emulsion stability.. Carbohydrate Polymers. A physicochemical investigation of two phosphatidylcholine/bile salt interfaces: Implications for lipase activation.. D. Formation of polysaccharides and protein multilayers. A. In M. & Lodge. P. 193–199. F. (1993). M. Journal of Agricultural and Food Chemistry. T. C. 63–71. J. Dickinson. Restoration of protein foam stability through electrostatic propylene glycol alginate-mediated protein–protein interactions. Munro. P. A fast standard instrument using computer image-analysis.. H. M. Food Hydrocolloids. & Dalgleish... Production and characterization of oil-in-water emulsions containing droplets stabilized by beta-lactoglobulin–pectin membranes.. & Wilde. J. Wilde. A. A. (1995). (1995). A. Wilde. Wilde. Arboleya... S. M. Colloids and Surfaces. (2003).. E. 167–175..J.. Hydration–dehydration properties of methylcellulose and hydroxypropylmethylcellulose. Miller. Parker.. (2004). The influence of surface composition and molecular diffusion on the stability of foams formed from protein detergent mixtures. R. H. (1996).. Nahringbauer. 91–98. 1. C.. FL: CRC Press. I. P. Dickinson. Colloids and Surfaces APhysicochemical and Engineering Aspects. R. L. 210. Thermoreversible gelation of aqueous methylcellulose solutions. 3930–3937. (1990). J. P. Colloids and Surfaces B-Biointerfaces.. Beaulieu. 6612–6617. & RajabiSiahboomi. 51(22).. P. Owusu. R. 32(21). P. Murray. A. (1992). D. 1–12. D. Colloids and Surfaces A-Physicochemical and Engineering Aspects. Polymer. Preparation of the emulsions and the factors affecting their stability. 20(3). (1999).. (1994). & Wilde. E. G. (2003). 15. Journal of Colloid and Interface Science. & Clark. B. (1996). L. (1984). B. 39–43. Mackie. 1580(2–3). Carbohydrate Polymers. J.. Dynamic surface tension of aqueous polymer solutions. Protein adsorption at solid–liquid interfaces: Reversibility and conformation aspects. Rheology of mixedcasein/-lactoglobulin films at the air–water interface. Competitive adsorption of b-lactoglobulin and b-casein with span 80 at the oil-water interface and the effects on emulsion behaviour. 1–13. R. N. Bemiller (Ed. & Daniels. Quimica Nova. G... Fang. P.. J. Hansen. S. & Dickinson.. 110–122. In J. & Smith. New York: Academic Press. L.. & Clark. J. 619–647). & Rammovsky. L.). N.. S. 8(4–5). J. 1. V. (2002). D. Dickinson. Damodaran. International Journal of Biological Macromolecules. D. Texture–structure relationships in foamed dairy emulsions. (2002). J. Rolfe. Colloids and Surfaces A-Physicochemical and Engineering Aspects. 865–866. F.. Macromolecules. D.. & Rodsrud. H. Wustneck. P. K. Mackie. Dickinson. Surface-tension by pendant drop. E. Food Research International. 49(2). (2000). P.. 197–210. D. Stanley. J. E. L. Methylcellulose and its derivatives. L. A. (1998).. & Clark.. 447–456. (2004). C. J.. E. 1–9. R.....).