Physicochemical Characters of a Tyrosinase Inhibitor Produced by Streptomyces roseolilacinus NBRC 12815

We examined the biological activities present in Streptomyces strains preserved at the National Institute of Technology and Evaluation Biological Resource Center, and found a metabolite of Streptomyces roseolilacinus NBRC 12815 that showed a potent anti-tyrosinase activity. The compounds with anti-t...

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Bibliographic Details
Published in:Biological & Pharmaceutical Bulletin 2009/05/01, Vol.32(5), pp.832-836
Main Authors: Nakashima, Takuji, Anzai, Kozue, Kuwahara, Natsumi, Komaki, Hisayuki, Miyadoh, Shinji, Harayama, Shigeaki, Tianero, Ma. Diarey Bordon, Tanaka, Junichi, Kanamoto, Akihiko, Ando, Katsuhiko
Format: Article
Language:English
Subjects:
Animals
Cell Line, Tumor
Cell Survival - drug effects
Chemical Phenomena
Dose-Response Relationship, Drug
Drug Stability
Enzyme Inhibitors - chemistry
Enzyme Inhibitors - isolation & purification
Enzyme Inhibitors - pharmacology
Melanins - biosynthesis
Mice
Molecular Conformation
Monophenol Monooxygenase - antagonists & inhibitors
secondary metabolite
Straptomyces roseolilacinus
Streptomyces
Streptomyces - metabolism
tyrosinase inhibitor
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Summary:We examined the biological activities present in Streptomyces strains preserved at the National Institute of Technology and Evaluation Biological Resource Center, and found a metabolite of Streptomyces roseolilacinus NBRC 12815 that showed a potent anti-tyrosinase activity. The compounds with anti-tyrosinase activity were purified by several chromatographic procedures. Final HPLC analysis revealed at least two anti-tyrosinase compounds with different retention times (12815A and B). The identification of two anti-tyrosinase compounds was performed with instrumental analysis and database search. The results obtained suggest that the active compounds are SF 2583A and B. Compound 12815A (IC50 values; about 9 μM) showed more potent tyrosinase inhibition than compound 12815B (IC50 values; about 1086 μM). The only structural difference between 12815A and B is the presence of an additional chloric atom. In addition, the activity of 12815A was markedly decreased under acidic conditions, resulting in irreversible inactivation. However, the inactivated 12815A still exhibited residual activity when exposed to detergent, Tween 80. These results suggest that the chlorine and the hydration water are very important in the exertion of anti-tyrosinase activity by 12815A.
ISSN:0918-6158
1347-5215
DOI:10.1248/bpb.32.832