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
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  • 英文篇名:Interaction between Unfolded Bovine β-Lactoglobulin and Epigallocatechin Gallate
  • 作者:付珊琳 ; 钟俊桢 ; 姚文俊 ; 覃芳芳 ; 刘成梅 ; 刘伟
  • 英文作者:FU Shanlin;ZHONG Junzhen;YAO Wenjun;QIN Fangfang;LIU Chengmei;LIU Wei;State Key Laboratory of Food Science and Technology, Nanchang University;
  • 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
  • 英文关键词:lactoglobulin(β-LG);;epigallocatechin gallate(EGCG);;fluorescence spectroscopy;;ultraviolet spectroscopy;;circular dichroism spectroscopy
  • 中文刊名:SPKX
  • 英文刊名:Food Science
  • 机构:南昌大学食品科学与技术国家重点实验室;
  • 出版日期:2018-05-15 16:04
  • 出版单位:食品科学
  • 年:2019
  • 期:v.40;No.593
  • 基金: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)
  • 语种:中文;
  • 页:SPKX201904003
  • 页数:7
  • CN:04
  • ISSN:11-2206/TS
  • 分类号:17-23
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(epigallocatechingallate,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。
        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 afterβ-lactoglobulin(β-LG) was treated by microwave. It was shown that EGCG could interact with β-LG or U-β-LG to formβ-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-LGEGCG 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.
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