食品科学 ›› 2019, Vol. 40 ›› Issue (4): 7-13.doi: 10.7506/spkx1002-6630-20171212-141

• 食品化学 • 上一篇    下一篇

去折叠态β-乳球蛋白与表没食子儿茶素没食子酸酯的相互作用

付珊琳,钟俊桢*,姚文俊,覃芳芳,刘成梅,刘?伟   

  1. (南昌大学 食品科学与技术国家重点实验室,江西?南昌 330047)
  • 出版日期:2019-02-25 发布日期:2019-03-05
  • 基金资助:
    国家自然科学基金地区科学基金项目(21366021);江西省自然科学基金青年项目(20161BAB214162); 江西省教育厅青年项目(150091);南昌大学食品科学与技术国家重点实验室青年研究基金项目(SKLF-QN-201518)

Interaction between Unfolded Bovine β-Lactoglobulin and Epigallocatechin Gallate

FU Shanlin, ZHONG Junzhen*, YAO Wenjun, QIN Fangfang, LIU Chengmei, LIU Wei   

  1. (State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang 330047, China)
  • Online:2019-02-25 Published:2019-03-05

摘要: 通过微波处理β-乳球蛋白(β-lactoglobulin,β-LG)得到去折叠态β-乳球蛋白(unfolded-β-lactoglobulin,U-β-LG),采用荧光光谱、紫外-可见光谱、圆二色光谱的方法研究表没食子儿茶素没食子酸酯(epigallocatechin gallate,EGCG)与U-β-LG的相互作用机制。结果表明,EGCG能与β-LG和U-β-LG相互作用形成复合物。它们相互之间均主要为疏水作用力。在298?K时,EGCG与β-LG和U-β-LG的结合距离分别为3.188?nm和2.875?nm。EGCG的结合使β-LG和U-β-LG的二、三级结构发生变化,表面疏水性降低。与天然β-LG相比,U-β-LG与EGCG具有更大的结合强度,结合后的U-β-LG发生更大的结构变化。

关键词: β-乳球蛋白, 表没食子儿茶素没食子酸酯, 荧光光谱, 紫外吸收光谱, 圆二色光谱

Abstract: The interaction mechanism of unfolded bovine β-lactoglobulin (U-β-LG) with epigallocatechin gallate (EGCG) was investigated by using fluorescence, ultraviolet and circular dichroism (CD) spectroscopy. U-β-LG was obtained after β-lactoglobulin (β-LG) was treated by microwave. It was shown that EGCG could interact with β-LG or U-β-LG to form β-LG-EGCG complex or U-β-LG-EGCG complex. The main binding force between EGCG and β-LG or U-β-LG was hydrophobic interaction. The binding distance between donor and acceptor at 298 K were 3.188 and 2.875 nm for β-LG-EGCG complex and U-β-LG-EGCG complex, respectively based on the F?rster’s theory of non-radiative energy transfer. The two- and three-dimensional structures of β-LG and U-β-LG were changed and their surface hydrophobicity was decreased slightly after being combined with EGCG. The binding affinity between U-β-LG and EGCG was stronger than that between β-LG and EGCG, which contributed to greater conformational change of U-β-LG.

Key words: β-lactoglobulin (β-LG), epigallocatechin gallate (EGCG), fluorescence spectroscopy, ultraviolet spectroscopy, circular dichroism spectroscopy

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