笃斯越橘花青素与牛血清白蛋白的相互作用

doi:10.7506/spkx1002-6630-201323002

食品科学 ›› 2013, Vol. 34 ›› Issue (23): 6-10.doi: 10.7506/spkx1002-6630-201323002

笃斯越橘花青素与牛血清白蛋白的相互作用

姚惠芳，景浩*

中国农业大学食品科学与营养工程学院，植物源功能食品北京市重点实验室，北京 100083

收稿日期:2012-09-16 修回日期:2013-10-30 出版日期:2013-12-15 发布日期:2014-01-03
通讯作者: 景浩 E-mail:hao.haojing@gmail.com
基金资助:
国家自然科学基金项目(31171676)

Spectroscopic Analysis of Interaction between Bovine Serum Albumin and Anthocyanin

YAO Hui-fang，JING Hao*

Beijing Key Laboratory of Functional Food from Plant Resources, College of Food Science and Nutritional Engineering,
China Agricultural University, Beijing 100083, China

Received:2012-09-16 Revised:2013-10-30 Online:2013-12-15 Published:2014-01-03
Contact: JING Hao E-mail:hao.haojing@gmail.com

摘要/Abstract

摘要：

采用荧光光谱、紫外-可见光谱和红外光谱法，研究笃斯越橘中花青素与牛血清白蛋白之间的相互作用。结果表明：花青素对牛血清白蛋白有较强的荧光猝灭作用且为静态猝灭，并计算得出不同温度下其结合常数(KA)与结合位点数(n)分别为：2.218×104、1.084(298K)，1.770×104、1.065(306K)，1.706×104、1.086(310K)。由热力学参数确定它们之间的作用力主要是静电引力，并根据Förster能量转移理论求得其结合距离为2.1nm。同步荧光光谱显示花青素主要与牛血清白蛋白中色氨酸残基发生相互作用，使其周围的疏水性增加。傅里叶变换红外光谱表明花青素可引起牛血清白蛋白的构象发生改变，使α-螺旋结构改变。

关键词: 花青素, 牛血清白蛋白, 荧光光谱, 紫外-可见光谱, 傅里叶变换红外光谱

Abstract:

The interaction between anthocyanin and bovine serum albumin (BSA) was studied by UV-Vis, fluorescence and
Fourier transform infrared spectroscopy (FT-IR). The results suggested that anthocyanin had a strong ability to quench the
BSA fluorescence in a static mode. The binding constants (KA) and site numbers (n) obtained at different temperatures were
2.218 × 104, 1.084 (298 K); 1.770 × 104, 1.065 (306 K) and 1.706 × 104, 1.086 (310 K), respectively. According to the
thermodynamic parameters, electrostatic forces played a dominant role in the interaction between anthocyanin and BSA. The
distance between donor and acceptor in anthocyanin-BSA complex was calculated as 2.1 nm, based on the equations from
Förster nonradiative energy transfer theory. The synchronous fluorescence spectra revealed that anthocyanin interacted with
tryptophan residues in BSA, and the vicinity of tryptophan residues was more hydrophobic. The FT-IR spectra revealed that
conformational changes of BSA were caused by anthocyanin, thus leading to structural changes of α-helix.

Key words: anthocyanin, bovine serum albumin, fluorescence spectroscopy, UV-Vis spectroscopy, Fourier transform infrared spectroscopy

中图分类号:

TS201.4

姚惠芳，景浩*. 笃斯越橘花青素与牛血清白蛋白的相互作用[J]. 食品科学, 2013, 34(23): 6-10.

YAO Hui-fang，JING Hao*. Spectroscopic Analysis of Interaction between Bovine Serum Albumin and Anthocyanin[J]. FOOD SCIENCE, 2013, 34(23): 6-10.

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笃斯越橘花青素与牛血清白蛋白的相互作用

Spectroscopic Analysis of Interaction between Bovine Serum Albumin and Anthocyanin

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