Study of the Self-Assembly and Aggregation Behavior of Temperature-Controlled Modified Glycinin and D-Galactose Colloidal Particles

Abstract

In this study, the mechanism of the temperature-induced self-assembly and aggregation of modified glycinin (denoted as S-11S) and D-galactose (DG) into complex colloidal particles was investigated at different temperatures based on their molecular structures and morphologies. Overall, high-temperature-treated S-11S and DG associate at cysteine and phenylalanine sites via ionic and disulfide bonds and self-assemble into colloidal particles of greater stability. And the self-assembly and aggregation behavior of molecules was regulated by temperatures. In addition, the sub-microstructure of the colloidal particles indicated that temperature can regulate the directional aggregation of complex colloidal particles. Rheological studies confirmed that the S-11S/DG colloidal particles formed network gel easily. Thus, the common heat-treated aggregation of the soy protein and its complex was evaluated to provide a new theoretical basis for the application of soy protein in gels and other areas and contribute to the design of new soy protein products.

Keywords: Temperature, Glycinin, D-galactose, self-assembly, Structure, Rheology