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Gewählte Publikation:

Gubitz, GM; Hayn, M; Urbanz, G; Steiner, W.
(1996): Purification and properties of an acidic beta-mannanase from Sclerotium rolfsii
J BIOTECHNOL. 1996; 45(2): 165-172. FullText FullText_BOKU

The plant pathogen basidiomycete Sclerotium rolfsii secretes five different beta-D-mannanases into the growth medium when cultivated in the presence of Amorphophallus konjak glucomannan as an inducer. Out of these enzymes an acidic endo-1,4-beta-mannanase was purified to electrophoretic homogeneity by means of ultrafiltration, anion exchange chromatography and gel filtration. This enzyme has a molecular mass of 61.2 kDa and the pI value is in the acidic region at 3.5. The pH and temperature optima are 2.9 and 74 degrees C, respectively, The mannanase is stable at low pH values and retains 50% of its activity after 4 h incubation at pH 3.0 and 50 degrees C. In addition to beta-1,4-linked mannans the mannanase of S. rolfsii also hydrolyzes glucomannans, galactomannans and manno-oligosaccharides not smaller than mannotetraose, but the enzyme does not show any mannosidase, xylanase, or endoglucanase activities. During the hydrolysis of mannotetraose in the presence of mannose, the monomer is transferred to other oligosaccharides, which has been proved by using C-14-labeled mannose.
Autor*innen der BOKU Wien:
Gübitz Georg

Find related publications in this database (Keywords)
Sclerotium rolfsii
acid stable

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