Abstract
To elucidate the mechanisms underlying the effects of glycinin (11S) and β-conglycinin (7S) on soy lipophilic protein (SLP) gel formation, it is essential to analyze the molecular interactions driving gelation, assess changes in protein physicochemical properties, and establish their correlations with the resulting gel characteristics. The formation of gels between 11S and SLP was facilitated by the presence of hydrogen and hydrophobic bonds, which enhanced the hydration and aggregation processes. When the ratio of 11S to SLP was 1:1, the hardness of SLP increased by 41.72 % to reach 886.73 gf. Similarly, 7S and SLP gels were driven by hydrogen and disulfide bonds, reducing aggregate size (93.76 ± 21.80 nm), increasing ζ-potential (-33.2 ± 4.56 mV) and solubility (50.09 ± 3.40 nm). Specifically, the elasticity of SLP increased by 12.61 % when 7S:SLP = 1:2. The hardness of the SLP gel can be adjusted by 11S, while the addition of 7S was responsible for adjusting the elasticity. 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 SLP gel.