Fabrication and characterization of succinylated and glycosylated soy protein isolate and its self-assembled nanogel

In this study, we used succinic anhydride (SA) acylation and dextran (DX) glycosylation modified soybean isolate protein (SPI) to develop self-assembled SPI-SA-DX adduct-based nanogels. Degree of modification, SDS-PAGE, and FT-IR studies showed that the amino group of the SPI was replaced by hydrophilic dextran and succinic acid carboxyl groups. Dextran chain and anhydride group attachment to the soybean protein surface enhanced hydrophilicity and spatial site blocking. Modification-induced protein structure unfolding, free sulfhydryl groups to be converted to disulfide bonds, and reduced surface hydrophobicity (H₀). H₀ was lowest at 33,750 ± 1008.29 when SA content = 10 % protein content (SPI-SA₃-DX). The nanometer gel based on SPI-SA₃-DX had the maximum turbidity and clear transparent solution without precipitation. Its particle size and polymer dispersibility index (PDI) were also the smallest, with values of (106.87 ± 4.51) nm and 0.21 ± 0.009, respectively. Transmission electron microscopy showed that nanogels had subspherical shell-core structures. Nanogels were stable under different pH, ionic strength, high temperature, and storage conditions.