摘要: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.