Degradation of cellulose and hemicelluloses by the brown rot fungus Piptoporus betulinus--production of extracellular enzymes and characterization of the major cellulases
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
17159214
DOI
10.1099/mic.0.29149-0
Knihovny.cz E-resources
- MeSH
- beta-Mannosidase metabolism MeSH
- Cellobiose metabolism MeSH
- Cellulases chemistry isolation & purification metabolism MeSH
- Cellulose 1,4-beta-Cellobiosidase metabolism MeSH
- Cellulose metabolism MeSH
- Endo-1,4-beta Xylanases metabolism MeSH
- Fungal Proteins chemistry isolation & purification metabolism MeSH
- Glucan 1,4-beta-Glucosidase biosynthesis MeSH
- Glucose metabolism pharmacology MeSH
- Enzyme Inhibitors pharmacology MeSH
- Isoelectric Point MeSH
- Kinetics MeSH
- Hydrogen-Ion Concentration MeSH
- Lignin metabolism MeSH
- Molecular Weight MeSH
- Oligosaccharides metabolism MeSH
- Polyporales enzymology metabolism MeSH
- Polysaccharides metabolism MeSH
- Triticum metabolism MeSH
- Carboxymethylcellulose Sodium metabolism MeSH
- Enzyme Stability MeSH
- Substrate Specificity MeSH
- Temperature MeSH
- Xylosidases metabolism MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- beta-Mannosidase MeSH
- Cellobiose MeSH
- Cellulases MeSH
- Cellulose 1,4-beta-Cellobiosidase MeSH
- Cellulose MeSH
- Endo-1,4-beta Xylanases MeSH
- exo-1,4-beta-D-xylosidase MeSH Browser
- Fungal Proteins MeSH
- Glucan 1,4-beta-Glucosidase MeSH
- Glucose MeSH
- hemicellulose MeSH Browser
- Enzyme Inhibitors MeSH
- Lignin MeSH
- lignocellulose MeSH Browser
- Oligosaccharides MeSH
- Polysaccharides MeSH
- Carboxymethylcellulose Sodium MeSH
- Xylosidases MeSH
Piptoporus betulinus is a common wood-rotting fungus parasitic for birch (Betula species). It is able to cause fast mass loss of birch wood or other lignocellulose substrates. When grown on wheat straw, P. betulinus caused 65% loss of dry mass within 98 days, and it produced endo-1,4-beta-glucanase (EG), endo-1,4-beta-xylanase, endo-1,4-beta-mannanase, 1,4-beta-glucosidase (BG), 1,4-beta-xylosidase, 1,4-beta-mannosidase and cellobiohydrolase activities. The fungus was not able to efficiently degrade crystalline cellulose. The major glycosyl hydrolases, endoglucanase EG1 and beta-glucosidase BG1, were purified. EG1 was a protein of 62 kDa with a pI of 2.6-2.8. It cleaved cellulose internally, produced cellobiose and glucose from cellulose and cellooligosaccharides, and also showed beta-xylosidase and endoxylanase activities. The K(m) for carboxymethylcellulose was 3.5 g l(-1), with the highest activity at pH 3.5 and 70 degrees C. BG1 was a protein of 36 kDa with a pI around 2.6. It was able to produce glucose from cellobiose and cellooligosaccharides, but also produced galactose, mannose and xylose from the respective oligosaccharides and showed some cellobiohydrolase activity. The K(m) for p-nitrophenyl-1,4-beta-glucoside was 1.8 mM, with the highest activity at pH 4 and 60 degrees C, and the enzyme was competitively inhibited by glucose (K(i)=5.8 mM). The fungus produced mainly beta-glucosidase and beta-mannosidase activity in its fruit bodies, while higher activities of endoglucanase, endoxylanase and beta-xylosidase were found in fungus-colonized wood.
References provided by Crossref.org
Enhancement of autofluorescence of the brown-rot fungus Piptoporus betulinus by metal ions