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Home > Literature List > Investigation of the interaction between (-)-epigallocatechin-3-gallate with trypsin and α-chymotrypsin

Investigation of the interaction between (-)-epigallocatechin-3-gallate with trypsin and α-chymotrypsin

Journal name:Food Science & Technology
Literature No.:
Literature Url: http://onlinelibrary.wiley.com/doi/10.1111/ijfs.12223/abstract?userIsAuthenticated=false&deniedAccessCustomisedMessage=
Date publication:12 JUL 2013

Abstract

Tea polyphenol (TP) inhibits digestive enzymes and reduces food digestibility. To explore the interaction between TP with digestive enzymes, bindings of -epigallocatechin-3-gallate (EGCG) to trypsin and α-chymotrypsin were studied in detail using fluorescence, resonance light-scattering, circular dichroism, fourier transform infrared spectroscopy methods and protein-ligand docking. The binding parameters were calculated according to Stern–Volmer equation, and the thermodynamic parameters were determined by the van't Hoff equation. The results indicated that EGCG was capable of binding trypsin and α-chymotrypsin with high affinity, resulting in a change of native conformation of these enzymes. EGCG had a greater influence on the structure of α-chymotrypsin than trypsin. This study can be used to

EGCG (with a purity of >99%) was purchased from Chengdu Biopurify Phytochemicals Ltd., Chengdu, China.