Effects of pH shift and D-galactose on network structure of glycinin gel and diffusion behavior of non-network proteins.

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 (mostly Glu and Asp), while the subunit B was the primary polypeptide forming the gel network.

Self-assembly and aggregation behavior of temperature-controlled modified glycinin and d-galactose colloidal particles.

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.