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Applied and Environmental Microbiology, March 1999, p. 1029-1035, Vol. 65, No. 3
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Purification and Characterization of a Novel Peroxidase from Geotrichum candidum Dec 1 Involved in Decolorization of Dyes

Seong Jun Kim and Makoto Shoda*

Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama 226-8503, Japan

Received 8 September 1998/Accepted 3 December 1998

A peroxidase (DyP) involved in the decolorization of dyes and produced by the fungus strain Geotrichum candidum Dec 1 was purified. DyP, a glycoprotein, is glycosylated with N-acetylglucosamine and mannose (17%) and has a molecular mass of 60 kDa and an isoelectric point (pI) of 3.8. The absorption spectrum of DyP exhibited a Soret band at 406 nm corresponding to a hemoprotein, and its Na2S2O4-reduced form revealed a peak at 556 nm that indicates the presence of a protoheme as its prosthetic group. Nine of the 21 types of dyes that were decolorized by Dec 1 cells were decolorized by DyP; in particular, anthraquinone dyes were highly decolorized. DyP also oxidized 2,6-dimethoxyphenol and guaiacol but not veratryl alcohol. The optimal temperature for DyP activity was 30°C, and DyP activity was stable even after incubation at 50°C for 11 h.

* Corresponding author. Mailing address: Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama 226-8503, Japan. Phone: 81-45-924-5274. Fax: 81-45-924-5276. E-mail: mshoda{at}res.titech.ac.jp.

Applied and Environmental Microbiology, March 1999, p. 1029-1035, Vol. 65, No. 3
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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