Mixed biopolymers at interfaces: Competitive adsorption and multilayer structures

Mixed biopolymer layers are commonly involved in the stabilization of food emulsions and foams. The interfacial composition and structure of mixed layers are predominantly determined by two mechanistic phenomena—competitive adsorption from mixed solution and cooperative adsorption into multilayers. The surface-active protein components typically dominate primary layers around droplets and bubbles, and the interacting polysaccharides form outer secondary stabilizing layers. This article reviews progress in understanding the factors controlling the nanoscale structure and physico-chemical properties of adsorbed layers in colloidal systems containing mixtures of biopolymers. Contributions from different experimental techniques are described, with particular attention directed towards the role of surface shear rheology in providing information on competitive adsorption of proteins and macromolecular interactions at fluid interfaces. We also consider here the phenomenon of phase separation in mixed protein monolayers, the balance of thermodynamic and kinetic factors in determining biopolymer layer properties, and the involvement of electrostatic interactions in the stabilization of emulsions by protein–polysaccharide complexes.