Affiliation:
1. Department of Applied Biological Chemistry, Graduate School of Agricultural Science, Kobe University, Rokko, Kobe 657-8501
2. Beauty Care Research Center, Kao Corporation, Bunka, Sumida-ku, Tokyo 131-8501, Japan
Abstract
ABSTRACT
Ceriporiopsis
sp. strain MD-1, isolated from forest soil, produced several extracellular enzymes that decolorized human hair melanin. Among them, three enzymes (E1, E2-1, and E2-2) were purified to homogeneity and characterized. The enzymes required hydrogen peroxide in their enzyme reactions and, typical of other fungal peroxidases, oxidized various phenol compounds such as guaiacol, but not 3,4-dimethoxybenzyl alcohol. The spectra of the three enzymes showed an absorption maximum at 406 nm, indicating that they were heme proteins. However, the
A
406
/
A
280
values of the enzymes were below 0.4, which was lower than those of other peroxidases. E2-1 and E2-2 were similar to each other in their molecular and catalytic properties, and they possibly represent products of posttranslational modifications and/or allelic variants of the same gene,
mdcA
. The corresponding cDNA was cloned and sequenced; the deduced amino acid sequence showed high identities to the manganese peroxidases from other microorganisms. The specific activities and
K
m
values of E2-1 and E2-2 for synthetic and human hair melanins were much higher than those of
Phanerochaete chrysosporium
manganese peroxidase and lignin peroxidase.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
Cited by
21 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献