Understanding of formation, gastrointestinal breakdown, and application of whey protein emulsion gels: Insights from intermolecular interactions.

Whey protein emulsion gel is an ideal model food for revealing how the multilength scale food structures affect food digestion, as their structure and mechanical properties can be precisely manipulated by controlling the type and intensity of intermolecular interactions between protein molecules. However, there are still significant understanding gaps among intermolecular interactions, protein aggregation and gelation, emulsion gel formation, gel breakdown in the gastrointestinal tract (GIT), and the practical use of whey protein emulsion gels, which limits their GIT-targeted applications. In this regard, the relationship between the structure and digestion behavior of heat-set whey protein emulsion gels is reviewed and discussed mainly from the following aspects: (1) structural characteristics of whey protein molecules; (2) how different types of intermolecular interactions influence heat-induced aggregation and gelation of whey protein in the aqueous solutions and the oil-in-water emulsions, and the mechanical properties of the final gels; (3) functions of the mouth, the stomach, and the small intestine in processing of solid foods, and how different types of intermolecular interactions influence the breakdown properties of heat-set whey protein emulsion gels in GIT (i.e., their respective role in controlling gel digestion). Finally, the implications of knowledge derived from the formation and gastrointestinal breakdown of heat-set whey protein emulsion gels for developing controlled delivery vehicles, human satiety enhancers, and sensory modifiers are highlighted.

Intermolecular forces regulate in-vitro digestion of whey protein emulsion gels: Towards controlled lipid release.

HYPOTHESIS: The utilization of emulsion-filled protein hydrogels for controlled lipid release in the gastrointestinal tract (GIT) displays great potential in drug delivery and obesity treatment. However, how intermolecular interactions among protein molecules influence lipid digestion of the gels is still understudied. EXPERIMENTS: Differently structured whey protein emulsion gels were fabricated by heating emulsions with blocking of disulfide bonds (the "noncovalent" gel), noncovalent interactions (the "disulfide" gel), or neither of these (the "control" gel). The intermolecular interactions-gel structure-lipid digestion relationship was investigated by characterizing structural/mechanical properties of the gels and monitoring their dynamic breakdown in a simulated GIT. FINDINGS: Although the disulfide-crosslinked protein network formed thick interfacial layers around oil droplets and resisted intestinal proteolysis, the "disulfide" gel had the fastest lipolysis rate, indicating that it could not inhibit the access of lipases to oil droplets. In contrast, the "noncovalent" gel was more susceptible to in-vitro digestion than the "control" gel because of lower gel strength, resulting in a faster lipolysis rate. This demonstrated that intermolecular disulfide bonds and noncovalent interactions played distinctive roles in the digestion of the gels; they represented the structural backbone and the infill in the gel structure, respectively.