Estimation of bound and free fractions of lignocellulose-degrading enzymes of wood-rotting fungi Pleurotus ostreatus, Trametes versicolor and Piptoporus betulinus
Language English Country France Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
16125911
DOI
10.1016/j.resmic.2005.06.004
PII: S0923-2508(05)00156-7
Knihovny.cz E-resources
- MeSH
- Cellulases analysis MeSH
- Cellulose metabolism MeSH
- Enzymes analysis MeSH
- Fungal Proteins analysis MeSH
- Glycoside Hydrolases analysis MeSH
- Culture Media chemistry MeSH
- Laccase analysis MeSH
- Lignin metabolism MeSH
- Freeze Drying MeSH
- Peroxidases analysis MeSH
- Pleurotus enzymology MeSH
- Polyporales enzymology MeSH
- Enzyme Stability MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Cellulases MeSH
- Cellulose MeSH
- Enzymes MeSH
- Fungal Proteins MeSH
- Glycoside Hydrolases MeSH
- hemicellulase MeSH Browser
- Culture Media MeSH
- Laccase MeSH
- Lignin MeSH
- lignocellulose MeSH Browser
- manganese peroxidase MeSH Browser
- Peroxidases MeSH
Liquid cultures with cellulose and solid state fermentation cultures on wheat straw of the white-rot fungi Pleurotus ostreatus and Trametes versicolor and the brown-rot fungus Piptoporus betulinus were assayed for the free and solid fraction-bound activity of lignocellulose-degrading enzymes. The majority of the ligninolytic enzymes laccase and Mn peroxidase was detected in the free fraction of P. ostreatus and T. versicolor. The endocleaving enzymes endo-1,4-beta-glucanase, endo-1,4-beta-mannanase and endo-1,4-beta-xylanase were detected almost exclusively in the free fraction, while significant amounts of 1,4-beta-glucosidase, cellobiohydrolase, 1,4-beta-xylosidase and 1,4-beta-mannosidase were present in the bound fraction depending on the mode of cultivation and the species. The bound enzymes accounted for 66% of the total activity in P. ostreatus straw cultures, 35% in T. versicolor and only 8% in P. betulinus. The enzymes also showed significant differences in freeze-drying stability. Hydrolases in general showed high stability, whereas laccase and Mn peroxidase of P. ostreatus were the least stable.
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