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  • 标题:Tyrosinase inhibition by p‐coumaric acid ethyl ester identified from camellia pollen
  • 本地全文:下载
  • 作者:Lijun Li ; Yuchen Cai ; Xu Sun
  • 期刊名称:Food Science & Nutrition
  • 电子版ISSN:2048-7177
  • 出版年度:2021
  • 卷号:9
  • 期号:1
  • 页码:389-400
  • DOI:10.1002/fsn3.2004
  • 出版社:John Wiley & Sons, Ltd.
  • 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.
  • 关键词:camellia pollen;inhibition;molecular docking;p‐coumaric acid ethyl ester;tyrosinase
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