Temperature affects the production, activity and stability of ligninolytic enzymes in Pleurotus ostreatus and Trametes versicolor
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
18298047
DOI
10.1007/bf02932110
Knihovny.cz E-resources
- MeSH
- Fungal Proteins chemistry metabolism MeSH
- Laccase chemistry metabolism MeSH
- Lignin metabolism MeSH
- Peroxidases metabolism MeSH
- Pleurotus enzymology growth & development MeSH
- Polyporales enzymology growth & development MeSH
- Enzyme Stability MeSH
- Temperature MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Fungal Proteins MeSH
- Laccase MeSH
- Lignin MeSH
- manganese peroxidase MeSH Browser
- Peroxidases MeSH
Enzyme activity was determined in cultures of Pleurotus ostreatus and Trametes versicolor with cellulose as a sole C source and high C/N ratio. The fungi were able to grow and produce laccase and Mn-peroxidase (MnP) at 5-35 degrees C, the highest production being recorded at 25-30 degrees C in P. ostreatus and at 35 degrees C in T. versicolor. Production of both enzymes at 10 degrees C accounted only for 4-20% of the maximum value. Temperature optima for enzyme activity were 50 and 55 degrees C for P. ostreatus and T. versicolor laccases, respectively, and 60 degrees C for MnP. Temperatures causing 50% loss of activity after 24 h were 32 and 47 degrees C for laccases and 36 and 30 degrees C for MnP from P. ostreatus and T. versicolor, respectively.
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