期刊
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
卷 51, 期 1-2, 页码 32-36出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.ijbiomac.2012.04.026
关键词
Tyrosinase; Naphthol; Monophenolase activity; Diphenolase activity; Inhibition kinetics
资金
- National Key Technology R&D Program of China [2007BAD07B06]
- Natural Science Foundation of China [31071611]
- Science and Technology Foundation of Fujian Province [2010N5013]
- National Foundation for Fostering Talents of Basic Science [J1030626]
Tyrosinase (EC 1.14.18.1), a copper-containing multifunctional oxidase, was known to be a key enzyme for biosynthesis in fungi, plants and animals. In this work, the inhibition properties alpha-naphthol and beta-naphthol toward the activity of tyrosinase have been evaluated, and the effects of alpha-naphthol and beta-naphthol on monophenolase and diphenolase activity of tyrosinase have been investigated. The results showed that both alpha-naphthol and beta-naphthol could potently inhibit both monophenolase activity and diphenolase activity of mushroom tyrosinase, and that beta-naphthol exhibited stronger inhibitory effect against tyrosinase than alpha-naphthol. For monophenolase activity, beta-naphthol could not only lengthen the lag time but also decrease the steady-state activity, while alpha-naphthol just only decreased the steady-state activity. For diphenolase activity, both alpha-naphthol and beta-naphthol displayed revisible inhibition. Kinetic analyses showed that both alpha-naphthol and beta-naphthol were competetive inhibitors. (c) 2012 Elsevier B.V. All rights reserved.
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