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Journal of Tea Science ›› 2022, Vol. 42 ›› Issue (6): 863-874.doi: 10.13305/j.cnki.jts.2022.06.001

• Research Paper • Previous Articles     Next Articles

Inhibitory Effect of Catechin Monomer EGC on Pancreatic Lipase and Mechanism

MAN Ziyi, FENG Yi, WU Xiangting*   

  1. College of Life and Environmental Science, Wenzhou University, Wenzhou 325035, China
  • Received:2022-06-30 Revised:2022-09-27 Online:2022-12-15 Published:2023-01-04

Abstract: In order to study the inhibitory effect and mechanism of epigallocatechin (EGC) on pancreatic lipase, EGC monomer was obtained from dry green tea by hot water extraction, chloroform depigmentation and column chromatography. The structure of purified EGC monomer was characterized by scanning electron microscope, Fourier transform infrared spectroscopy and 1H-NMR spectroscopy. The inhibitory effect and types of EGC on pancreatic lipase were studied by titration, and the effect of EGC on pancreatic lipase structure was characterized by fluorescence spectroscopy and molecular docking. The results show that EGC exhibited the inhibition on pancreatic lipase in a non-competitive manner. The inhibitory effect continued to rise with the increase of EGC concentration, and the half inhibitory concentration (IC50) was (1.62±0.085) mg·mL-1. There was a fluorescence quenching effect of EGC on pancreatic lipase. EGC could bind to amino acid residues in the enzyme through intermolecular hydrogen bonds and hydrophobic interactions, resulting in the changes in chemical structure and spatial conformation of the enzymes, thus decreasing the enzyme activity. The results show that EGC mainly inhibited the activity of pancreatic lipase by changing the chemical structure and spatial conformation of pancreatic lipase, so as to achieve the hypolipidemic effect.

Key words: epigallocatechin, pancreatic lipase, intermolecular hydrogen bonds, mechanism

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