Implication of Dichomitus squalens manganese-dependent peroxidase in dye decolorization and cooperation of the enzyme with laccase
Language English Country United States Media print-electronic
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
- MeSH
- Anthraquinones metabolism MeSH
- Azo Compounds metabolism MeSH
- Bacterial Proteins isolation & purification metabolism MeSH
- Color MeSH
- Coloring Agents metabolism MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Laccase isolation & purification metabolism MeSH
- Lignin metabolism MeSH
- Molecular Weight MeSH
- Mycology methods MeSH
- Naphthalenesulfonates metabolism MeSH
- Oxidation-Reduction MeSH
- Peroxidases isolation & purification metabolism MeSH
- Polyporaceae enzymology MeSH
- Triticum MeSH
- Drug Synergism MeSH
- Trypan Blue metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- Anthraquinones MeSH
- Azo Compounds MeSH
- Bacterial Proteins MeSH
- Coloring Agents MeSH
- C.I. Reactive Violet 5 MeSH Browser
- Laccase MeSH
- Lignin MeSH
- lignocellulose MeSH Browser
- manganese peroxidase MeSH Browser
- Naphthalenesulfonates MeSH
- Peroxidases MeSH
- pontamine sky blue MeSH Browser
- reactive orange 16 MeSH Browser
- Remazol Brilliant Blue R MeSH Browser
- Trypan Blue MeSH
Three new chromatographic forms of Dichomitus squalens manganese-dependent peroxidase (MnP) were isolated from wheat-straw cultures using Mono Q and connective interaction media (CIM) fast protein liquid chromatography. Enzymes revealed identical molar mass of 50 kDa (estimated by SDS-PAGE) and pI values of 3.5, however, they varied in Km values obtained for Mn2+ oxidation. The addition of wood and straw methanol extracts to the cultures showed that the production of MnPs in wheat-straw cultures was influenced rather by the type of cultivation than by phenolic compounds from lignocellulosic material which induced laccase production. The purified CIM1 MnP was able to decolorize selected azo and anthraquinone dyes more rapidly than laccase Lc1. In vitro dye decolorization showed a synergistic cooperation of MnP and laccase. In the case of CSB degradation MnP prevented from the production of a differently colored substance that could be produced after CSB degradation by laccase-HBT system.
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