化学
大豆蛋白
贮藏蛋白
没食子酸表没食子酸酯
猝灭(荧光)
无规线圈
没食子酸
食品科学
生物物理学
生物化学
蛋白质二级结构
荧光
多酚
核化学
抗氧化剂
基因
物理
量子力学
生物
作者
Guo Huang,Hainan Jin,Guichen Liu,Shuyuan Yang,Lianzhou Jiang,Yan Zhang,Xiaonan Sui
出处
期刊:Food Chemistry
[Elsevier]
日期:2022-11-01
卷期号:394: 133484-133484
被引量:15
标识
DOI:10.1016/j.foodchem.2022.133484
摘要
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.
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