Decolorization of industrial dyes by a Brazilian strain of Pleurotus pulmonarius producing laccase as the sole phenol-oxidizing enzyme
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
12094737
DOI
10.1007/bf02817651
Knihovny.cz E-resources
- MeSH
- Coloring Agents metabolism MeSH
- Fermentation MeSH
- Laccase MeSH
- Oxidoreductases biosynthesis metabolism MeSH
- Pleurotus enzymology metabolism MeSH
- Industrial Microbiology * MeSH
- Monophenol Monooxygenase biosynthesis metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Geographicals
- Brazil MeSH
- Names of Substances
- Coloring Agents MeSH
- Laccase MeSH
- Oxidoreductases MeSH
- Monophenol Monooxygenase MeSH
The ability of a Brazilian strain of Pleurotus pulmonarius to decolorize structurally different synthetic dyes (including azo, triphenylmethane, heterocyclic and polymeric dyes) was investigated in solid and submerged cultures. Both were able to decolorize completely or partially 8 of 10 dyes (Amido Black, Congo Red, Trypan Blue, Methyl Green, Remazol Brilliant Blue R, Methyl Violet, Ethyl Violet, Brilliant Cresyl Blue). No decolorization of Methylene Blue and Poly R 478 was observed. Of the four phenol-oxidizing enzymes tested in culture filtrates (lignin peroxidase, manganese peroxidase, aryl alcohol oxidase, laccase), P. pulmonarius produced only laccase. Both laccase activity and dye decolorization were related to glucose and ammonium starvation or to induction by ferulic acid. The decolorization in vivo was tested using three dyes--Remazol Brilliant Blue R, Trypan Blue and Methyl Green. All of them were completely decolorized by crude extracellular extracts. Decolorization and laccase activity were equally affected by pH and temperature. Laccase can thus be considered to be the major enzyme involved in the ability of P. pulmonarius to decolorize industrial dyes.
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