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• The modified glycinin (S-11S) is complexed with d -galactose (DG). • Heat promotes the covalent interaction of S-11S and DG at Cys and Phe sites. • The structure of the S-11S/DG colloidal particles is altered by heating. • Temperature affects the aggregation behavior of the S-11S/DG colloidal particles. • The S-11S/DG colloidal particles formed network gel easily. The molecular structure and morphologies of complex colloidal particles with modified glycine (S-11S) and d -galactose were studied by multispectral, microscopic imaging and chromatographic techniques at different temperatures, and the self-assembly and aggregation mechanisms were determined. Overall, high-temperature-treated S-11S and d -galactose associate at cysteine and phenylalanine sites and self-assemble into colloidal particles of greater stability than glycinin and S-11S via ionic and disulfide bonds. The structure and subunit content of composite colloidal particles were changed. Assessing the sub-microstructure reveals that temperature can regulate the directional aggregation of complex colloidal particles. The elasticity of the complex colloidal particles is maximum enhanced at 95 ℃ as confirmed by the rheological. Thus, the 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. [ABSTRACT FROM AUTHOR]

To reduce the content of non-network proteins in protein-based gels, a synergistic approach involving pH shift and D-galactose (DG) was developed herein to obtain elastic gels with dense networks. The results revealed that the combined effect of pH shift and DG promoted the formation of additional disulfide bonds and chemical bonds between molecules, resulting in a denser, and highly elastic gel network, which immobilized more aggregates, leading to a significant reduction in non-network protein content, and enhancing the functional properties of the gel. Moreover, non-network proteins primarily consisted of subunit A 4 (mostly Glu and Asp), while the subunit B was the primary polypeptide forming the gel network. Therefore, the removal of the non-network protein has no significant effect on the microstructure, water holding capacity, elasticity, and recovery of the gel. Comprehensively, the combination of pH shift and DG generated a positive synergistic effect of the glycinin hydrogel network structure., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024. Published by Elsevier Ltd.)