Gel Properties of Soy Protein Isolate Modified by Lipoxygenase-Catalyzed Linoleic Acid Oxidation and Their Influence on Pepsin Diffusion and In Vitro Gastric Digestion.

The model of lipoxygenase-catalyzed linoleic acid (LA) oxidation was selected as representative of a lipid peroxidation system to investigate the effects of oxidative modification on soybean protein isolate (SPI) gel properties and in vitro gastric digestion. Fluorescence recovery after the photobleaching (FRAP) technique was applied to evaluate pepsin diffusion in the gel. The results showed that oxidative modification increased the gel hardness as well as brought about a compact and three-dimensional network structure, which consequently decreased the water mobility as manifest by lowering the relaxation time of T2b and T21 from 0.55 and 3.22 ms for the control to 0.32 and 2.42 ms for 7LA+LOX (addition of 7 mL of LA and LOX), respectively. It was interesting to note that pepsin diffusion was significant correlated (p < 0.05) with T2b and DH (degree of hydrolysis), indicating that water mobility might be a factor related to FITC-pepsin diffusion, which would ultimately influence the gel gastric digestion. Compared with native SPI, moderate oxidation can improve the digestibility of SPI gel by the summed effects of pepsin diffusion limitation, microstructure variation, and hydrolysis degree.