食品科学 ›› 2008, Vol. 29 ›› Issue (6): 104-107.

• 基础研究 • 上一篇    下一篇

柿子单宁对牛血清白蛋白的荧光猝灭作用研究

 顾海峰, 梁晋鄂, 李春美, 徐玉娟, 陈美红, 胡婉峰   

  1. 华中农业大学食品科技学院; 中国食品工业协会; 华中农业大学食品科技学院;广东省农业科学院蚕业与农产品加工研究所; 广东省果蔬深加工重点实验室
  • 出版日期:2008-06-15 发布日期:2011-08-26

Fluorescence Quench to Bovine Serum Albumin by Persimmon Tannin

 GU  Hai-Feng, LIANG  Jin-E, LI  Chun-Mei, XU  Yu-Juan, CHEN  Mei-Hong, HU  Wan-Feng   

  1. 1.College of Food Science and Technology, Huazhong Agricultural University; 2. Food Industry Associations of China; 3. Sericulture and Farm Produce Processing Research Institute, Guangdong Academy of Agricultural Sciences, Key Laboratory of Guangdong for Deep Processing of Fruits and Vegetables
  • Online:2008-06-15 Published:2011-08-26

摘要: 采用荧光光谱和紫外吸收光谱法研究了柿子单宁对牛血清白蛋白(BSA)的荧光猝灭作用。结果表明,柿子单宁可以有规律地使BSA内源荧光猝灭,其猝灭机理可认为是柿子单宁与BSA形成复合物的静态猝灭,并获得了不同温度下柿子单宁与BSA作用的结合常数和热力学参数。根据所得结果可推断柿子单宁与BSA的作用力为疏水作用力和静电作用力,同时由Forster非辐射能量转移理论计算得出了柿子单宁与BSA结合位置的距离。

关键词: 柿子单宁, 牛血清白蛋白, 相互作用, 荧光猝灭

Abstract: The interaction between persimmon tannin and bovine serum albumin (BSA) and the mechanism of fluorescence quench were studied by fluorescence spectroscopy and ultraviolet-visible absorption spectroscopy. The results showed that the fluorescence of BSA is quenched regularly by persimmon tannin. The binding constants and thermodynamic parameters of persimmon tannin with BSA are obtained at different temperatures. The hydrophobic interaction force and electrostatic force play a main role in the binding of persimmon tannin with BSA. The distances of binding site between persimmon tannin and BSA are also obtained according to the theory of Forster’s non-radiative energy transfer.

Key words: persimmon tannin, bovine serum albumin (BSA), interaction, fluorescence quench