Abstract
Factors affecting the structure and composition of adsorbed protein layers are described with reference to macroscopic oil-water interfaces and protein-stabilized oil-in-water emulsions. Measurements of specular neutron reflectance and surface shear viscosity provide information on differences in adsorbed layers between the disordered β-casein and globular proteins such as β-lactoglobulin or bovine serum albumin. Recent studies of competitive adsorption and co-operative interfacial interactions are described for systems containing binary mixtures of proteins, mixtures of proteins and surfactants, and mixtures of proteins and polysaccharides. The relationship of adsorbed layer structure to emulsion stability is discussed.
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