Physicochemical Changes and in Vitro Gastric Digestion of Modified Soybean Protein Induced by Lipoxygenase Catalyzed Linoleic Acid Oxidation.

Abstract

Protein oxidation results in structural modification which affects its digestion. The objective of this work was to investigate the influence of lipoxygenases (LOX) catalyzed linoleic acid (LA) oxidation on the structure and in vitro gastric digests of soybean protein isolate (SPI). Fluorescence recovery after photobleaching (FRAP) was used to evaluate the relationship between pepsin diffusion and gastric digestion. Results indicated that oxidation induced carbonyl formation and loss of free sulfhydryl. Increased surface hydrophobicity and zeta-potential verified the protein unfolding and thus resulted in a small particle size and low fluorescence intensity. Fourier transform infrared spectroscopy (FTIR) showed that oxidation caused the increases in β-sheets mostly at the expense of α-helix and random coils. Fluorescein isothiocyanate (FITC)-pepsin in SPI solution modified with 3 mL LA showed a faster diffusion rate with 80.51 μm2/s as well as a higher DH value of 9.11%, showing that pepsin diffusivity might play an important role in protein gastric digestion.