Estimation of bound and free fractions of lignocellulose-degrading enzymes of wood-rotting fungi Pleurotus ostreatus, Trametes versicolor and Piptoporus betulinus
Jazyk angličtina Země Francie Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
16125911
DOI
10.1016/j.resmic.2005.06.004
PII: S0923-2508(05)00156-7
Knihovny.cz E-zdroje
- MeSH
- celulasy analýza MeSH
- celulosa metabolismus MeSH
- enzymy analýza MeSH
- fungální proteiny analýza MeSH
- glykosidhydrolasy analýza MeSH
- kultivační média chemie MeSH
- lakasa analýza MeSH
- lignin metabolismus MeSH
- lyofilizace MeSH
- peroxidasy analýza MeSH
- Pleurotus enzymologie MeSH
- Polyporales enzymologie MeSH
- stabilita enzymů MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- celulasy MeSH
- celulosa MeSH
- enzymy MeSH
- fungální proteiny MeSH
- glykosidhydrolasy MeSH
- hemicellulase MeSH Prohlížeč
- kultivační média MeSH
- lakasa MeSH
- lignin MeSH
- lignocellulose MeSH Prohlížeč
- manganese peroxidase MeSH Prohlížeč
- peroxidasy 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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