In situ interaction of pea peptides and bile salts under in vitro digestion: Potential impact on lipolysis

[Display omitted] •Pea protein peptides (PPP) do not constitute a barrier to the interfacial penetration of bile salts (BS)•Gastric residence time influences the ability of BS to solubilize oleic acid in duodenal conditions.•The supramolecular assemblies PPP-BS solubilize more fatty acid than BS micelles.•The extent of lipolysis is maximum in the presence of PPP.•Bioaccesibility of healthy fatty acids increases in the presence of PPP. The present work evaluated how a native pea protein isolate (PPI) affects the key roles carried out by bile salts (BS) in lipid digestion by means of the in vitro static INFOGEST protocol. Two gastric residence times were evaluated (10 and 60 min), and then the peptides obtained (GPPP) were mixed with BS at physiological concentration in simulated intestinal fluid to understand how they interact with BS both at the bulk and at the interface. Both GPPP give rise to a film with a predominant viscous character that does not constitute a barrier to the penetration of BS, but interact with BS in the bulk duodenal fluid. When the peptides flushing from the stomach after the different gastric residence times undergo duodenal digestion, it was found that for the longer gastric residence time the percentage of soluble fraction in the duodenal phase, that perform synergistically with BS micelles, was twice that of the lower residence time, leading to an increase in the solubilization of oleic acid. These results finally lead to a greater extent of lipolysis of olive oil emulsions. This work demonstrates the usefulness of in vitro models as a starting point to study the influence of gastric residence time of pea protein on its interaction with BS, affecting lipolysis. Pea proteins were shown to be effective emulsifiers that synergistically perform with BS improving the release and bioaccessibility of bioactive lipids as olive oil.