Decolorization of sulfonphthalein dyes by manganese peroxidase activity of the white-rot fungus Phanerochaete chrysosporium
Language English Country United States Media print
Document type Journal Article
PubMed
15058190
DOI
10.1007/bf02931512
Knihovny.cz E-resources
- MeSH
- Enzyme Activation drug effects MeSH
- Sodium Azide pharmacology MeSH
- Coloring Agents metabolism MeSH
- Chelating Agents pharmacology MeSH
- Cysteine pharmacology MeSH
- Edetic Acid pharmacology MeSH
- Phenolphthaleins metabolism MeSH
- Enzyme Inhibitors pharmacology MeSH
- Colorimetry MeSH
- Environmental Pollutants metabolism MeSH
- Peroxidases antagonists & inhibitors metabolism MeSH
- Phanerochaete enzymology MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Sodium Azide MeSH
- Coloring Agents MeSH
- Chelating Agents MeSH
- Cysteine MeSH
- Edetic Acid MeSH
- Phenolphthaleins MeSH
- Enzyme Inhibitors MeSH
- Environmental Pollutants MeSH
- manganese peroxidase MeSH Browser
- Peroxidases MeSH
Manganese peroxidase (MnP) was produced by shallow stationary cultures of Phanerochaete chrysosporium growing on N-limited medium. Decolorization of sulfonphthalein (SP) dyes by MnP was investigated. The MnP activity profile and decolorization of SP dyes was correlated and almost all dyes were decolorized at pH 4.0. The influence of various inhibitors on Bromocresol Purple decolorization suggested an oxidative nature of the MnP-catalyzed decolorization of SP dyes.
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