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

Kim, Seong Jun, Shoda, Makoto·1999·Applied and Environmental Microbiology
DOI 10.1128/aem.65.3.1029-1035.1999
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Abstract

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 Na 2 S 2 O 4 -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.

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Metadata

Authors
Kim, S. J., & Shoda, M.
Venue
Applied and Environmental Microbiology
Publisher
American Society for Microbiology
Published
1999-03
Volume
65
Issue
3
Pages
1029-1035
ISSN
  • 0099-2240
  • 1098-5336
DOI
10.1128/aem.65.3.1029-1035.1999
Cited by
274
References
0
Language
en
Licence
journals.asm.org/non-commercial-tdm-license (tdm)

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