Due to the bound protein, the conjugate is much more surface-active than the polysaccharide on its own; hence the conjugate is able to achieve surface layer saturation at a much lower bulk concentration. At the same time, due to the covalently bound polysaccharide, the adsorbed protein layer is protected against destabilization under unfavourable environmental conditions (e.g., heating, low pH, high electrolyte concentrations, etc.). The large size and hydrophilicity of the polysaccharide moiety generates long-range steric repulsion between emulsion droplets surfaces. Theoretical calculations have recently shown (Ettelaie, Akinshina, & Dickinson, in press) that a strong association of a specific part of a moderately large polysaccharide entity (>5–10 kDa) to an adsorbing protein can confer sufficient additional steric stabilization to overcome any surface–surface attractive interaction that might be present with the adsorbed protein alone under unfavourable conditions of pH and/or ionic strength. While this interfacial biopolymer structure is most efficiently realised with a permanent covalent linkage, a more common situation in food emulsion systems is where protein–polysaccharide complexation arises from non-covalent association driven by electrostatic interactions