| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1233287 | Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy | 2011 | 5 Pages |
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.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► The binding interaction of (−)-epigallocatechin (EGC) with bovine β-lactoglobulin (βLG) was investigated. ► The negative entropy change and the enthalpy change indicated that the interaction of EGC and βLG was driven mainly by van der Waals interactions and hydrogen bonding. ► This also indicated that the surface of βLG was covered by EGC, resulting in change of native conformation of βLG. ► Our study may be helpful for further elucidation of binding interactions of green tea flavanoids with milk proteins.
