The binding mechanisms between soy β-conglycinin/glycinin and (−)-epigallocatechin-3-gallate (EGCG) were evaluated using multi-spectral techniques and molecular modeling. Additionally, the emulsifying properties of β-conglycinin/glycinin were investigated in their interactions with EGCG. Fluorescence analysis revealed that the quenching of β-conglycinin/glycinin by EGCG was static quenching. Specifically, EGCG to β-conglycinin/glycinin resulted in the conformation changes of the Trp and Tyr residues, around which the polarity toward more hydrophilic. The dominated binding between β-conglycinin and EGCG was hydrogen bonding, whereas was mainly hydrophobic force between glycinin and EGCG. Such affinity induced a more organized protein confirmation with decreased random coil and increased α-helix and β-structures. The docking data indicated the better affinity between glycinin and EGCG, compared to β-conglycinin. The emulsifying ability and capacity of β-conglycinin were enhanced with involvement EGCG, however no effect was found for glycinin. Our findings deliver insights in understanding of the interaction mechanisms between β-conglycinin/glycinin and EGCG.

使用多光谱技术和分子建模评估了大豆 β-伴大豆球蛋白/大豆球蛋白和 (-)-表没食子儿茶素-3-没食子酸酯 (EGCG) 之间的结合机制。此外，研究了 β-伴大豆球蛋白/大豆球蛋白与 EGCG 相互作用的乳化特性。荧光分析表明EGCG对β-伴大豆球蛋白/大豆球蛋白的猝灭是静态猝灭。具体来说，EGCG 到 β-伴大豆球蛋白/大豆球蛋白导致 Trp 和 Tyr 残基的构象发生变化，其周围的极性更趋于亲水。β-伴大豆球蛋白和EGCG之间的主要结合是氢键，而大豆球蛋白和EGCG之间主要是疏水力。这种亲和力通过减少无规卷曲和增加α-螺旋和β-结构来诱导更有组织的蛋白质确认。对接数据表明，与 β-伴大豆球蛋白相比，大豆球蛋白和 EGCG 之间的亲和力更好。EGCG参与后β-伴大豆球蛋白的乳化能力和乳化能力增强，但对大豆球蛋白无影响。我们的研究结果为理解 β-伴大豆球蛋白/大豆球蛋白与 EGCG 之间的相互作用机制提供了见解。