Isolation of 6-hydroxy-<scp>l</scp>-tryptophan from the fruiting body of <i>Lyophyllum decastes</i> for use as a tyrosinase inhibitor

DOI PDF 被引用文献2件 オープンアクセス
  • Atsushi Ishihara
    Faculty of Agriculture, Tottori University, Tottori, Japan
  • Naomi Sugai
    Faculty of Agriculture, Tottori University, Tottori, Japan
  • Tomohiro Bito
    Faculty of Agriculture, Tottori University, Tottori, Japan
  • Naoki Ube
    The United Graduate School of Agricultural Sciences, Tottori University, Tottori, Japan
  • Kotomi Ueno
    Faculty of Agriculture, Tottori University, Tottori, Japan
  • Yasuhito Okuda
    The Tottori Mycological Institute, The Japan Kinoko Research Center Foundation, Tottori, Japan
  • Emi Fukushima-Sakuno
    The Tottori Mycological Institute, The Japan Kinoko Research Center Foundation, Tottori, Japan

書誌事項

公開日
2019-10-03
権利情報
  • https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model
DOI
  • 10.1080/09168451.2019.1621157
公開者
Informa UK Limited

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<jats:title>ABSTRACT</jats:title> <jats:p>Tyrosinase is the key enzyme that controls melanin formation. We found that a hot water extract of the lyophilized fruiting body of the fungus Lyophyllum decastes inhibited tyrosinase from Agaricus bisporus. The extract was fractionated by ODS column chromatography, and an active compound was obtained by purification through successive preparative HPLC using an ODS and a HILIC column. Using spectroscopic data, the compound was identified to be an uncommon amino acid, 6-hydroxytryptophan. 6-Hydroxy-l-tryptophan and 6-hydroxy-d-tryptophan were prepared through a Fenton reaction from l-tryptophan and d-tryptophan, respectively. The active compound was determined to be 6-hydroxy-l-tryptophan by comparison of their circular dichroism spectra and retention time on HPLC analysis of the Nα-(5-fluoro-2,4-dinitrophenyl)-l-leuciamide derivative with those of 6-hydroxy-l-tryptophan and 6-hydroxy-d-tryptophan. A Lineweaver–Burk plot of the enzyme reaction in the presence of 6-hydroxy-l-tryptophan indicated that this compound was a competitive inhibitor. The IC50 values of 6-hydroxy-l-tryptophan was 0.23 mM.</jats:p>

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