Polysaccharide-water interface

Three polysaccharide-water interfaces are shown in Fig. 1. The agarose interface is observed to be indifferent to water (Hayashi and Kanzaki, 1987), judging from its distinctly sharp, hydrophobic boundary. The methylcellu-lose and pectin boundaries are diffuse and clearly hydrophilic. The air bubbles on methylcellulose attest to its efficacy as a foam stabilizer. The interfaces depicted in Fig. 1 can be visualized on a macromolecular scale as the interfaces between dispersed polysaccharide molecules and water. 

Polysaccharides interfaced with water act as adsorbents on which surface accumulations of solute lower the interfacial tension. The polysaccharide-water interface is a dynamic site of competing forces. Water retains heat longer than most other solvents. The rate of accumulation of micromolecules and microions on the solid surface is directly proportional to their solution concentration and inversely proportional to temperature. As adsorbates, micromolecules and microions ordinarily adsorb to an equilibrium concentration in a monolayer (positive adsorption) process they desorb into the outer volume in a negative adsorption process. The adsorption-desorption response to temperature of macromolecules—including polysaccharides —is opposite that of micromolecules and microions. As adsorbate, polysaccharides undergo a nonequilibrium, multilayer accumulation of like macromolecules. 

Owing to the diverse chemical nature of functional groups in proteins and polysaccharides, they are prone to a variety of types of molecular interactions, both in bulk aqueous media and at air-water or oil-water interfaces. To a first approximation one may consider an adsorbed layer of biopolymers at the interface as simply a special type of highly concentrated biopolymer solution. Thus, the same variety of interactions that are typically found for biopolymers in a bulk aqueous media also occur in biopolymer adsorbed layers at the interfaces in food colloids. Moreover, these same molecular interactions are also involved in the close encounters between pairs of colloidal particles covered by adsorbed biopolymer layers. In the rest of this chapter we shall briefly remind ourselves of the main basic types of intermolecular interactions readers requiring more detailed background information are directed to other sources (Cantor and Schimmel, 1980 Lehninger, 1982 Israelachvili, 1992 Dickinson, 1998 Finkelstein and Ptitsyn, 2002 McClements, 2005, 2006 Min et al., 2008). 

Antipova, A., Semenova, M., Gauthier-Jacques, A. (1997). Effect of neutral carbohydrate structure on protein surface activity at air-water and oil-water interfaces. In Dickinson, E., Bergenstahl, B. (Eds). Food Colloids Proteins, Lipids and Polysaccharides, Cambridge, UK Royal Society of Chemistry, pp. 245-258. 

Thermodynamically unfavourable interactions between two biopolymers may produce a significant increase in the surface shear viscosity (rf) of the adsorbed protein layer. This change in surface rheological behaviour is a consequence of the greater surface concentration of adsorbed protein. For instance, with p-casein + pectin at pH = 5.5 and ionic strength = 0.01 M (Ay = 2.6 x 10 m3 mol kg-2), the surface shear viscosity at the oil-water interface was found to increase by 20-30%, i.e., rp = 750 75 and 590 60 mN s m-1 in the presence and absence of polysaccharide. These values of rp refer to data taken some 24 hours following initial protein layer formation (Dickinson et al., 1998 Semenova et al., 1999a). 

The presence of a thermodynamically favourable interaction between protein and polysaccharide is commonly associated with a marked decrease in protein surface activity at the air-water or oil-water interface (see Figures 7.5b and 7.15). There is a slower decay in the surface tension for complexes in comparison with the pure protein, and also higher values of the tension in the steady state. Data establishing these trends have been reported for the following biopolymer pairs in aqueous media legumin + dextran and legumin + maltodextrin (Antipova and Semenova,... 

Figure 7.15 Effect of thermodynamically favourable interactions between biopolymers on protein surface activity at the planar oil-water or air-water interface. The surface pressure n reached after 6 hours is plotted against the polysaccharide concentration ( ), legumin (0.001 wt%) + dextran (Mw = 270 kDa) at / -decane-water surface at pH = 7.8 and ionic strength = 0.01 M, (Ay = -0.2 x 105 cm3 mol1) (Pavlovskaya et ah, 1993) ( ), legumin (0.001 wt%) + maltodextrin (MD6, Mw = 102 kDa) at air-water surface at pH = 7.2 and ionic strength = 0.05 M (Ay = - 0.02 x 105 cm3 mol-1) (Belyakova et ah, 1999) (A), legumin (0.001 wt%) + maltodextrin (MD10, Mw = 45 kDa) at air-water surface at pH = 7.2 and ionic strength = 0.05 M (.1 / = - 0.08 x 105 cm3 mol-1) (Belyakova et ah, 1999).

Surface shear rheology at the oil-water interface is a sensitive probe of protein-polysaccharide interactions. In particular, there is considerable experimental evidence for a general increase in surface shear viscosity of protein adsorbed layers as a result of interfacial complexation with polysaccharides (Dickinson et al., 1998 Dickinson and Euston, 1991 Dickinson and Galazka, 1992 Semenova et al., 1999a Jourdain et al., 2009). One such example is the case of asi-casein + pectin at pH = 5.5 and ionic strength = 0.01 M (Ay = - 334 x 10 cm /mol) the interfacial viscosity after 24 hours was found to be five times larger in the presence of pectin (i.e., values of 820 80 and 160 20 mN m 1 with and without pectin, respectively) (Semenova et al., 1999a). 

Ganzevles, R.A., Cohen Stuart, M.A., van Vliet, T., de Jongh, H.H.J. (2006). Use of polysaccharides to control protein adsorption to the air-water interface. Food Hydrocoll-oids, 20, 872-878. 

In general, surface activity behaviour in food colloids is dominated by the proteins and the low-molecular-weight surfactants. The competition between proteins and surfactants determines the composition and properties of adsorbed layers at oil-water and air-water interfaces. In the case of mixtures of proteins with non-surface-active polysaccharides, the resulting surface-activity is usually attributed to the adsorption of protein-polysaccharide complexes. By understanding relationships between the protein-protein, protein-surfactant and protein-polysaccharide interactions and the properties of the resulting adsorbed layers, we can aim to... 

Figure 8.12 illustrates the effect of complex formation between protein and polysaccharide on the time-dependent surface shear viscosity at the oil-water interface for the system BSA + dextran sulfate (DS) at pH = 7 and ionic strength = 50 mM. The film adsorbed from the 10 wt % solution of pure protein has a surface viscosity of t]s > 200 mPa s after 24 h. As the polysaccharide is not itself surface-active, it exhibited no measurable surface viscosity (t]s < 1 niPa s). But, when 10 wt% DS was introduced into the aqueous phase below the 24-hour-old BSA film, the surface viscosity showed an increase (after a further 24 h) to a value around twice that for the original protein film. Hence, in this case, the new protein-polysaccharide interactions induced at the oil-water interface were sufficiently strong to influence considerably the viscoelastic properties of the adsorbed biopolymer layer. 

In another set of studies, it has been reported that the in vitro digestibility of lipid droplets by pancreatic lipase is significantly affected by emulsifier type (Mun et al, 2006, 2007 Park et al., 2007). Intuitively, one might expect that a thick dense layer of strongly bound protein-polysaccharide complex at the oil-water interface would reduce considerably the in vivo accessibility of lipases, and hence would reduce the rate of human metabolism of fats. Establishment of the validity of this hypothesis must still await consolidation of a substantial body of detailed results from independent systematic studies on a broad range of mixed biopolymer systems. 

Figure 8.15 Cartoon showing how proteins, polysaccharides and surfactants (emulsifiers) might be distributed at the triglyceride-water interface. Inter-facial complexation in vivo between adsorbed protein and charged polysaccharide in the gastrointestinal tract could affect digestion of protein and fat by forming structures that inhibit the accessibility and activity of enzymes (proteases and lipases). Reproduced from Dickinson (2008) with permission.

Baeza, R., Sanchez, C.C., Pilosof, A.M.R., Rodriguez Patino, J.M. (2005). Interactions of polysaccharides with p-lactoglobulin adsorbed films at the air-water interface. Food Hydrocolloids, 19, 239-248. 

In Part Four (Chapter eight) we focus on the interactions of mixed systems of surface-active biopolymers (proteins and polysaccharides) and surface-active lipids (surfactants/emulsifiers) at oil-water and air-water interfaces. We describe how these interactions affect mechanisms controlling the behaviour of colloidal systems containing mixed ingredients. We show how the properties of biopolymer-based adsorption layers are affected by an interplay of phenomena which include selfassociation, complexation, phase separation, and competitive displacement. 

Because of their large interfacial area, emulsions are basically unstable. In order to produce a stable emulsion, a surfactant is mostly needed. The surfactants are adsorbed at the oil-water interface, forming a link between the two phases of different polarity. For this purpose, a wide variety of emulsifying agents is currently available. Polysaccharides such as arabic gum, tragacanth, Karaya gum, and different seaweed carbohydrate polymers have been employed. They, however, show considerable batch-to-batch variations and might support microbial growth. 

Several studies have been made of LB films of esters of naturally occurring polysaccharides. Kawaguchi et al. [242] formed long chain esters of cellulose which, however, could only be formed into multilayers by the horizontal lifting technique. Schoondorp et al. [243] studied LB multilayers of esters of amylose and showed that materials with short alkyl side chains have a helical conformation at the air/water interface and that this structure can be transferred into multilayers. As in the case of the isotactic polymethylmethacrylate, the helical structure appears to lead to an oriented structure in the LB film. These two families of materials are illustrated in Figure 5.9. 

Microbial mats and biofilms, defined as surface layers of microbes entrained in a matrix of extracellular polymeric substances (EPS) (Characklis and Marshall, 1989), are also important in changing the surface texture and erodibility of sediments in estuaries (de Beer and Kiihl, 2001). The EPS are primarily composed of cellular-derived polysaccharides, polyuronic acids, proteins, nucleic acids, and lipids (Decho and Lopez, 1993 Schmidt and Ahring, 1994). The EPS can serve as a cementing agent for surface sediment particles, thereby affecting the erodibility of sediments as well as the flux of dissolved constituents across the sediment-water interface (de Beer and Kiihl, 2001). 

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