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

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 i

SUBMITTER: Li L 

PROVIDER: S-EPMC7802545 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature