Analysis of binding interaction between (-)-epigallocatechin (EGC) and β-lactoglobulin by multi-spectroscopic method.

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.