Open AccessTyrosinase inhibition by p ‐coumaric acid ethyl ester identified from camellia pollen
Author(s) -
Li Lijun,
Cai Yuchen,
Sun Xu,
Du Xiping,
Jiang Zedong,
Ni Hui,
Yang Yuanfan,
Chen Feng
Publication year - 2021
Publication title -
food science and nutrition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.614
H-Index - 27
ISSN - 2048-7177
DOI - 10.1002/fsn3.2004
Subject(s) - tyrosinase , arbutin , chemistry , p coumaric acid , chromatography , nuclear chemistry , solvent , enzyme , stereochemistry , biochemistry , ferulic acid
A tyrosinase inhibitor was separated from camellia pollen with the aid of solvent fraction, macroporous adsorptive resin chromatography, and high‐speed countercurrent chromatography. The inhibitor was identified to be p ‐coumaric acid ethyl ester ( p ‐CAEE) by nuclear magnetic resonance and mass spectrum. Its inhibitory activity (IC 50 = 4.89 μg/ml) was about 10‐fold stronger than arbutin (IC 50 = 51.54 μg/ml). The p ‐CAEE inhibited tyrosinase in a noncompetitive model with the K I and K m of 1.83 μg/ml and 0.52 mM, respectively. Fluorescence spectroscopy analysis showed the p ‐CAEE quenched an intrinsic fluorescence tyrosinase. UV‐Vis spectroscopy analysis showed the p ‐CAEE did not interact with copper ions of the enzyme. Docking simulation implied the p‐ CAEE induced a conformational change in the catalytic region and thus changed binding forces of L‐tyrosine. Our findings suggest that p ‐CAEE plays an important role in inhibiting tyrosinase and provides a reference for developing pharmaceutical, cosmetic, and fruit preservation products using pollen.