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Position: Home > Articles > Interaction between β-Lactoglobulin and Black Rice Anthocyanin FOOD SCIENCE 2017,38 (9) 85-90

β-乳球蛋白与黑米花色苷的相互作用

作  者:
赵焕焦;吕晓玲;王梦姝;王璐瑶
单  位:
天津科技大学食品工程与生物技术学院
关键词:
黑米花色苷;β-乳球蛋白;荧光光谱;紫外吸收光谱;抗氧化性;分子对接
摘  要:
从荧光光谱、同步荧光光谱、紫外-可见光谱、抗氧化能力和分子对接等方面,研究黑米花色苷(black rice anthocyanin,BRA)与β-乳球蛋白(β-lactoglobulin,β-LG)在模拟生理条件下的相互作用。结果显示,BRA对β-LG具有较强的荧光猝灭,猝灭方式为静态猝灭,说明二者发生相互结合,同时计算了结合位点数和结合常数,热力学参数表明疏水作用力为其主要的作用力;根据非辐射能量转移理论,结合距离r为3.14 nm。同步荧光光谱结果显示,BRA与β-LG的相互作用影响乳球蛋白的构象,但不影响色氨酸和酪氨酸的微环境;分子对接结果显示BRA中的主要成分矢车菊-3-O-葡萄糖苷与β-LG的结合主要是疏水作用力,该结果与热力学参数分析结果相一致。
译  名:
Interaction between β-Lactoglobulin and Black Rice Anthocyanin
作  者:
ZHAO Huanjiao;Lü Xiaoling;WANG Mengshu;WANG Luyao;College of Food Engineering and Biotechnology,Tianjin University of Science and Technology;
关键词:
black rice anthocyanin(BRA);;β-lactoglobulin(β-LG);;fluorescence spectroscopy;;ultraviolet spectroscopy;;antioxidant capacity;;molecular docking
摘  要:
In this work, we studied the interaction between black rice anthocyanin(BRA) and β-lactoglobulin(β-LG) by fluorescence spectroscopy, synchronous fluorescence spectroscopy, ultraviolet-visible spectroscopy, antioxidant capacity and molecular docking under simulated physiological conditions. The results showed that black rice anthocyanin had a strong ability to quench the fluorescence of β-lactoglobulin in a static mode. The binding constants(Ka) and site numbers(n) were obtained at different temperatures. The major interaction force was hydrophobic interaction in the binding of BRA to β-lactoglobulin based on the thermodynamic parameters. According to F?rster's non-radiative energy transfer theory, the donor-acceptor proximity in BRA-β-LG complex was calculated as 3.14 nm. The synchronous fluorescence spectra revealed that interaction with BRA caused conformational changes in β-LG, but did not affect the microenvironment of tryptophan and tyrosine residues. Molecular docking indicated that the main driving force of the interaction between cyaniding-3-O-glucoside(the major component of black rice anthocyanin) and β-lactoglobulin was hydrophobic interaction, which was consistent with the result obtained from thermodynamic parameter analysis.

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