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- W2106603721 abstract "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." @default.
- W2106603721 created "2016-06-24" @default.
- W2106603721 creator A5051615779 @default.
- W2106603721 creator A5084505187 @default.
- W2106603721 date "1999-03-01" @default.
- W2106603721 modified "2023-10-03" @default.
- W2106603721 title "Purification and Characterization of a Novel Peroxidase from <i>Geotrichum candidum</i> Dec 1 Involved in Decolorization of Dyes" @default.
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- W2106603721 doi "https://doi.org/10.1128/aem.65.3.1029-1035.1999" @default.
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