Fungal laccases - occurrence and properties
Language English Country England, Great Britain Media print
Document type Journal Article, Research Support, Non-U.S. Gov't, Review
PubMed
16472305
DOI
10.1111/j.1574-4976.2005.00010.x
PII: FMR010
Knihovny.cz E-resources
- MeSH
- Biotechnology methods MeSH
- Fungal Proteins chemistry metabolism MeSH
- Fungi enzymology MeSH
- Laccase chemistry classification metabolism MeSH
- Environment MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Review MeSH
- Names of Substances
- Fungal Proteins MeSH
- Laccase MeSH
Laccases of fungi attract considerable attention due to their possible involvement in the transformation of a wide variety of phenolic compounds including the polymeric lignin and humic substances. So far, more than a 100 enzymes have been purified from fungal cultures and characterized in terms of their biochemical and catalytic properties. Most ligninolytic fungal species produce constitutively at least one laccase isoenzyme and laccases are also dominant among ligninolytic enzymes in the soil environment. The fact that they only require molecular oxygen for catalysis makes them suitable for biotechnological applications for the transformation or immobilization of xenobiotic compounds.
References provided by Crossref.org
Production of laccase enzyme from Curvularia lunata MY3: purification and characterization
Laccases and Tyrosinases in Organic Synthesis
Involvement of laccase-like enzymes in humic substance degradation by diverse polar soil bacteria
Yeast Hosts for the Production of Recombinant Laccases: A Review
Development of soil microbiology methods: from respirometry to molecular approaches
Autofluorescence of the fruiting body of the fungus Macrolepiota rhacodes