Interfacial structure and stability of food emulsions as affected by protein–polysaccharide interactions

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Abstract
The exploitation of protein–polysaccharide interactions offers opportunities for the design of new ingredients and interfacial structures with applications in the food and pharmaceutical industries. Association of protein and polysaccharide molecules may occur chemically through covalent bonds or physically through electrostatic interactions. Theoretical and experimental studies indicate that various molecular and thermodynamic factors can be adjusted to optimize the effectiveness of covalent conjugates and electrostatic complexes in the stabilization of interfaces, gels and emulsions. Maillard-type protein–polysaccharide conjugates have excellent emulsifying and steric stabilizing properties, especially under conditions where the protein alone is poorly soluble. Charged polysaccharides form soluble complexes or coacervates with proteins depending on pH, ionic strength, and biopolymer charge distribution. The structure and stabilizing properties of the mixed protein + polysaccharide layer depends on the sequence of adsorption of the biopolymers to the interface. There is good potential for use of interfacial protein–polysaccharide complexes in the nanoscale engineering of delivery vehicles for nutrient encapsulation and in the protection of adsorbed proteins and emulsified lipids against enzymatic breakdown during digestion.