Analysis of the gel properties, microstructural characteristics, and intermolecular forces of soybean protein isolate gel induced by transglutaminase.

Abstract

Soybean protein isolate (SPI) is a high‐quality plant protein that is primarily used to process various soybean products coagulated by transglutaminase (TGase). In this study, the degree of hydrolysis (DH), sulfhydryl content (SH), surface hydrophobicity (H0 ), secondary structural constitution, and microstructure of TGase‐treated soybean protein (SPI, 7S, and 11S) were determined, as well as the effects of NaCl, urea, and SDS on the properties and intermolecular forces of SPI gel were analyzed. The results show that the H0 and SH content of SPI, 7S, and 11S decreased significantly with TGase treatment time (p < .05), while the DH gradually increased and reached its highest value (3.72%, 7.41%, and 1.27%, respectively) at 30 min. As the concentration of these two secondary structures exhibited an inverse relationship, the degradation of β‐turns resulted in the increase in β‐sheets. The microstructures of SPI and 11S gels were similar, being denser and more ordered than 7S gel. The low concentration of NaCl solution (0.2 mol/L) enhanced gel properties and intermolecular forces, promoting the formation of SPI gel, whereas a high concentration (0.4–0.8 mol/L) had a significant inhibitory effect. Urea and SDS solutions substantially inhibited the formation of SPI gel, leading to significant decreases in the water holding capacity and hardness as well as a considerable increase in the coagulation time (p < .05). The results revealed that hydrogen bonds and hydrophobic interactions were the main intermolecular forces responsible for the gel formation. This study provides adequate technical support and a theoretical basis for soybean protein gel products.