Impact of non-covalent bound polyphenols on conformational, functional properties and in vitro digestibility of pea protein

[Display omitted] •Interaction mechanism between PPI and three polyphenols was investigated.•EGCG, CA and RES induced conformational changes in the PPI structure.•Non-covalent binding of PPI with polyphenols improved its functional properties.•Polyphenols changed the in vitro digestive properties of pea protein. This study investigated the effects of the non-covalent interaction of pea protein isolate (PPI) with epigallocatechin-3-gallate (EGCG), chlorogenic acid (CA) and resveratrol (RES) on the structural and functional properties of proteins. The conformational changes of the protein structure with EGCG, CA and RES were analyzed using fourier transform infrared spectroscopy. Polyphenols strongly quenched the intrinsic fluorescence of PPI mainly through static quenching. The main interaction force was hydrogen bonding and van der Waals forces for PPI-EGCG, the main interaction force of PPI-CA complex was electrostatic interaction, while RES and PPI were bound by hydrophobic interaction. Free sulfhydryl groups and surface hydrophobicity significantly decreased in PPI after binding with phenolic compounds. The presence of EGCG, CA and RES enhanced the emulsification, foaming and in vitro digestibility of PPI. These results illustrate the potential applications of PPI-polyphenol complexes in food formulations.