Changes in the structure and functional properties of soybean isolate protein: Effects of different modification methods

Abstract

Soybean protein isolate (SPI) is an important plant protein in food processing; however, its spherical structure prevents the exposure of its hydrophobic residues and affects its functional properties. In this study, we elucidate the effects of deamidation, phosphorylation, and glycosylation on the structure (Fourier-transform infrared spectroscopy, circular dichroism, fluorescence, and scanning electron microscopy) and functional properties (solubility, emulsifying activity index (EAI), and emulsifying stability index (ESI)) of SPI. The zeta potentials of the deamidated, phosphorylated, and glycosylated (DSPI, PSPI, and MSPI, respectively) samples decreased significantly (p < 0.05) relative to those of SPI. The functional properties of the modified SPI samples were improved, with MSPI-2 showing the best solubility (86.73 ± 0.34%), EAI (118.89 ± 0.73 m2/g), and ESI (273.33 ± 0.59 min). Moreover, the effects of the three modifications on the SPI functional properties increase in the order MSPI > PSPI > DSPI. These results provide a theoretical understanding the relationship between the modifications and SPI structure.