College of Light Industry and Food Science, South China University of Technology, Guangzhou, Guangdong Province 510642, PR China.
Spectrochim Acta A Mol Biomol Spectrosc. 2011 Nov;82(1):164-8. doi: 10.1016/j.saa.2011.07.028. Epub 2011 Jul 20.
The binding interaction between (-)-epigallocatechin (EGC) with bovine β-lactoglobulin (βLG) was investigated by fluorescence, circular dichroism (CD) and Fourier transform infrared (FTIR) spectroscopy methods. The binding parameters were determined by Stern-Volmer equation and the thermodynamic parameters were calculated according to the van't Hoff equation. The results suggested that βLG was bound by EGC, which resulted in change of native conformation of βLG. van der Waals interactions and hydrogen bonding probably played major roles in the binding process. Our study is helpful for further elucidation of binding interactions between catechins with milk proteins, which would contribute to the development of novel milk products.
采用荧光光谱、圆二色光谱（CD）和傅里叶变换红外光谱（FTIR）等方法研究了（-）-表没食子儿茶素没食子酸酯（EGC）与牛β-乳球蛋白（βLG）之间的结合相互作用。通过 Stern-Volmer 方程确定了结合参数，并根据 van't Hoff 方程计算了热力学参数。结果表明，βLG 与 EGC 结合，导致βLG 天然构象发生变化。范德华相互作用和氢键可能在结合过程中起主要作用。我们的研究有助于进一步阐明儿茶素与乳蛋白之间的结合相互作用，这将有助于开发新型乳制品。
