Proteins and emulsifiers at liquid interfaces

The interfacial properties of proteins and emulsifiers have been studied extensively in the field of food colloid research. Emulsions form the basis of a huge range of food products and are generally stabilised by either protein and/or emulsifiers. Proteins have been shown to stabilise emulsions by forming a viscoelastic, adsorbed layer on the oil droplets, which form a physical barrier to coalescence. Emulsifiers can be oil or water soluble, forming a fluid, close-packed layer at the interface with a low interfacial tension. This results in an emulsion with a small droplet size distribution, stabilised by the fluid Gibbs–Marangoni mechanism or weak electrostatic repulsion. In real food emulsions, there is usually a mixture of proteins and emulsifiers competing for the interfacial area. This can produce a finer emulsion, however, the emulsifiers break down the viscoelastic protein-adsorbed layer, resulting in an emulsion with reduced stability. We present a review recent work that aims to characterise the composition, structure and physical properties of mixed protein–emulsifier interfaces, in an effort to understand the mechanisms behind the stability behaviour of food emulsion systems.