Interfacial design of protein-stabilized emulsions for optimal delivery of nutrients

Abstract

Proteins are often used as ingredients in food emulsions, as their amphiphilic structures provide electrostatic and steric stabilization. Significant attention has recently been directed at understanding how the composition and structure of oil–water interfaces change during digestion and how these can be manipulated to enhance the delivery of nutrients contained within the oil droplets. These efforts have necessitated the development of more sophisticated in vitro digestion models of greater physiological relevance and increased efforts in research to identify the role of the various digestive parameters on interfacial dynamics. The changes occurring at the oil–water interface will affect the adsorption of gastro-intestinal lipases and, ultimately, affect lipid digestion. The composition of a protein-stabilized oil droplet changes continuously during digestion, because of proteolysis and the formation of peptides with different affinities for the interface. In addition, natural bio-surfactants such as phospholipids and bile salts, other surface- active molecules present in foods, and the products of lipolysis (i.e. mono and diglycerides, lysophospholipids), all compete for access to the interface, and contribute to the dynamic changes occurring on the surface of the oil droplets. A better understanding of how to tailor the composition of oil droplet surfaces in food emulsions will aid in optimizing lipid digestion and, as a result, delivery of lipophilic nutrients. This review focuses on the physico-chemical changes occurring in protein-stabilized oil-in-water emulsions during gastric and small intestine digestion, and on how interfacial engineering could lead to differences in fatty acid release and the potential bioavailability of lipophilic molecules.