The chemistry behind the antioxidant actions of soy protein isolate hydrolysates in a liposomal system: Their performance in aqueous solutions and liposomes.

Soy protein isolate (SPI) and its derived hydrolysates (SPIHs) are popular food ingredients due to their demonstrated antioxidant, stabilizing and emulsifying properties. However, little is known about the interplays among these functions. This study aimed to fill this knowledge gap through comparing the antioxidant activities in single-phase assays systems and biphasic liposomal systems of the SPIHs produced by pepsin, trypsin or alcalase with/without flavourzyme. The peptide fraction of SPIHs with molecular weight < 1 kDa generally contributed more to the detected antioxidant activity. The combination hydrolysis of flavourzyme with pepsin/trypsin/alcalase significantly influenced SPIH's reducing power and Fe2+ chelating capacity. In liposomal systems, SPIHs influenced positively system's stability while inhibiting primary and secondary lipid oxidation products. Besides the factors affecting SPIH's antioxidant activity in the aqueous system (like amino acid composition, sequence and peptide chain length), interactions of peptides/amino acids with liposomal membrane and its lipid components also played critical roles.