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Structural criteria for depigmenting mechanism of arbutin
Author(s) -
Hori Ikuyo,
Nihei Kenichi,
Kubo Isao
Publication year - 2004
Publication title -
phytotherapy research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.019
H-Index - 129
eISSN - 1099-1573
pISSN - 0951-418X
DOI - 10.1002/ptr.1456
Subject(s) - arbutin , hydroquinone , ascorbic acid , cofactor , chemistry , oxygen , substrate (aquarium) , tyrosinase , biochemistry , biology , organic chemistry , enzyme , food science , ecology
Arbutin, hydroquinone‐ O ‐ β ‐ d ‐glucopyranoside (1) was found to inhibit the oxidation of l ‐tyrosine (monophenolase activity) catalyzed by mushroom tyrosinase. However, arbutin itself was oxidized as a monophenol substrate at an extremely slow rate, and this oxidation was accelerated as soon as catalytic amounts (0.01 m m ) of l ‐3,4‐dihydroxyphenylalanine ( l ‐DOPA) became available as a cofactor. The result observed was supported by monitoring oxygen consumption. The depigmenting mechanism of arbutin previously reported is supportable if a cofactor is not available in the melanocytes. The combination with l ‐ascorbic acid is a useful application, particularly when oxygen is limited. Copyright © 2004 John Wiley & Sons, Ltd.