Purification and characterization of a novel peroxidase from Geotrichum candidum dec 1 involved in decolorization of dyes.
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 degrees C, and DyP activity was stable even after incubation at 50 degrees C for 11 h.
Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama 226-8503, Japan.
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Kim
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Shoda
D000880:Anthraquinones / Q000378:metabolism; D001391:Azo Compounds / Q000378:metabolism; D001673:Biodegradation, Environmental; D004396:Coloring Agents / Q000378:metabolism*; D004795:Enzyme Stability; D005848:Geotrichum / Q000201:enzymology* / Q000302:isolation & purification; D006861:Hydrogen Peroxide / Q000494:pharmacology; D007700:Kinetics; D010544:Peroxidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D012988:Soil Microbiology; D013379:Substrate Specificity; D013696:Temperature
D000880:Anthraquinones; D001391:Azo Compounds; D004396:Coloring Agents; D006861:Hydrogen Peroxide; D010544:Peroxidases