Isolation of 6-hydroxy-l -tryptophan from the fruiting body of Lyophyllum decastes for use as a tyrosinase inhibitor
| Autor: | Tomohiro Bito, Naoki Ube, Kotomi Ueno, Yasuhito Okuda, Naomi Sugai, Atsushi Ishihara, Emi Fukushima-Sakuno |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
0301 basic medicine
chemistry.chemical_classification Mushroom biology Chemistry Tyrosinase Organic Chemistry Tryptophan Lyophyllum decastes General Medicine Fungus biology.organism_classification Applied Microbiology and Biotechnology Biochemistry Tyrosinase inhibitor Analytical Chemistry 03 medical and health sciences 030104 developmental biology 0302 clinical medicine Enzyme Agaricus 030220 oncology & carcinogenesis Molecular Biology Biotechnology |
| Zdroj: | Bioscience, Biotechnology, and Biochemistry. 83:1800-1806 |
| ISSN: | 1347-6947 0916-8451 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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