Mushroom tyrosinase inhibitory activity of esculetin isolated from seeds of euphorbia lathyris L

Yukimitsu Masamoto, Hideya Ando, Yoshiyuki Murata, Yasuaki Shimoishi, Mikiro Tada, Kyoya Takahata

Research output: Contribution to journalArticle

149 Citations (Scopus)

Abstract

A tyrosinase inhibitor was isolated from the seeds of Euphorbia lathyris L. by bioassay-guided fractionation and purification, using silica gel column chromatography. It was identified as esculetin by comparing its physical properties and spectral data with those of an authentic sample. The IC50 value of esculetin in the mushroom tyrosinase activity test was 43 μM. The kinetic study indicates that esculetin exhibited competitive inhibition against the oxidation of 3-(3,4-dihydroxyphenyl)-alanine by mushroom tyrosinase. The structure-activity relationships among five esculetin analogs suggest that hydroxyl groups at the C6 and C7 positions of the coumarin skeleton played an important role in the expression of tyrosinase inhibitory activity.

Original languageEnglish
Pages (from-to)631-634
Number of pages4
JournalBioscience, Biotechnology and Biochemistry
Volume67
Issue number3
DOIs
Publication statusPublished - Jan 1 2003

Keywords

  • Coumarin
  • Esculetin
  • Euphorbia lathyris L
  • Mushroom tyrosinase inhibitory activity

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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