关键词: β-伴大豆球蛋白, 大豆球蛋白, 表没食子儿茶素没食子酸酯（EGCG）, 相互作用

Abstract: The interaction between β-conglycinin (7S)/glycinin (11S) and epigallocatechin gallate (EGCG) under neutral conditions was characterized by fluorescence spectroscopy, UV-Vis spectroscopy, Fourier transform infrared spectroscopy and molecular docking. The results showed that EGCG and 7S/11S could interact with each other at pH 7.0, which induced a change in the microenvironment of amino acid residues. EGCG could quench the intrinsic fluorescence of 7S/11S by dynamic and static methods. EGCG has higher affinity to 11S than 7S. The reaction between EGCG and 7S/11S were a spontaneous binding process, which mainly formed a 1:1 complex at molar ratio by hydrogen bond and van der Waals force. EGCG could reduce the surface hydrophobicity of 7S/11S. With the increasing of EGCG concentration, the change of 11S became more obvious. Fourier transform infrared spectroscopy and molecular docking studies suggested that in addition to hydrogen bonds, hydrophobic interactions were also involved in the formation of complexes. The binding of EGCG could lead to different changes in the secondary structure of 7S/11S, subsequently resulting in protein unfolding.

Key words: β-conglycinin (7S), glycinin (11S), epigallocatechin gallate (EGCG), interaction