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Investigation of the interaction between (−)‐epigallocatechin‐3‐gallate with trypsin and α‐chymotrypsin
Author(s) -
Wu Xuli,
He Weiyi,
Wang Wenpu,
Luo Xinpin,
Cao Heyao,
Lin Lixia,
Feng Kaiqian,
Liu Zhigang
Publication year - 2013
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/ijfs.12223
Subject(s) - chymotrypsin , trypsin , chemistry , circular dichroism , epigallocatechin gallate , gallate , enzyme , biochemistry , crystallography , polyphenol , nuclear chemistry , antioxidant
Summary 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 S tern– V olmer equation, and the thermodynamic parameters were determined by the van't H off 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 explain the binding interaction mechanism between TP and digestive enzymes.