Physicochemical and Gelling Properties of Gels Formed by Soy Lipophilic Protein with Β-Conglycinin and Glycinin

Abstract

To understand the effect of glycinin (11S) and β-conglycinin (7S) on soy lipophilic protein (SLP) gel formation, it's important to analyse protein properties such as composition, particle size, ζ-potential and solubility. The study investigated structural and gel properties including texture, rheology, water distribution, microstructure and intermolecular forces. Gels formed between 11S and SLP were strengthened by hydrogen and hydrophobic bonds, improving hydration and aggregation. When 11S:SLP = 1:1, SLP hardness increased by 41.72% to 886.73 N. Similarly, 7S and SLP gels were driven by hydrogen and disulfide bonds, reducing aggregate size and increasing ζ-potential, solubility and gel viscosity. Specifically, the elasticity of SLP increased by 12.61% when SLP = 1:2. The interaction between 11S, 7S and SLP was based on hydrophobic interactions and α-helix for protein folding and water binding. Principal component analysis showed that 11S had a significant influence on the properties in the 11S-7S-SLP gel.

Keywords: soy lipophilic protein, β-conglycinin, globulin, interactions, gels