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  3. Tyrosinase inhibition by p-coumaric acid ethyl ester identified from camellia pollen

Tyrosinase inhibition by p-coumaric acid ethyl ester identified from camellia pollen

  • Food Sci Nutr. 2020 Dec 11;9(1):389-400. doi: 10.1002/fsn3.2004.
Lijun Li 1 2 3,  Yuchen Cai 1,  Xu Sun 1,  Xiping Du 1 2 3,  Zedong Jiang 1 2 3,  Hui Ni 1 2 3,  Yuanfan Yang 1 2 3,  Feng Chen 1 4
Affiliations

Affiliations

  • 1 College of Food and Biological Engineering Jimei University Xiamen China.
  • 2 Fujian Provincial Key Laboratory of Food Microbiology and Enzyme Engineering Xiamen China.
  • 3 Research Center of Food Biotechnology of Xiamen City Xiamen China.
  • 4 Department of Food, Nutrition and Packaging Sciences Clemson University Clemson SC USA.
PMID: 33473301 DOI: 10.1002/fsn3.2004
Abstract

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 (IC50 = 4.89 μg/ml) was about 10-fold stronger than arbutin (IC50 = 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.

Keywords

camellia pollen; inhibition; molecular docking; p‐coumaric acid ethyl ester; tyrosinase.

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