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Purification and mo...
Purification and mode of action of a low molecular mass endo-1,4-β-d-glucanase from Fusarium oxysporum
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Christakopoulos, Paul (författare)
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- Kekos, D. (författare)
- National Technical University of Athens
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- Macris, B.J. (författare)
- National Technical University of Athens
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- Claeyssen, M. (författare)
- Universiteit of Gent
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- Bhat, M.K. (författare)
- Institute of Food Research, Reading
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(creator_code:org_t)
- Elsevier BV, 1995
- 1995
- Engelska.
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Ingår i: Journal of Biotechnology. - : Elsevier BV. - 0168-1656 .- 1873-4863. ; 39:1, s. 85-93
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- A low molecular mass (23.2 kDa) endo-1,4-β-d-glucanase from Fusarium oxysporum was purified to homogeneity by gel-filtration and ion-exchange chromatographies. The enzyme was optimally active at pH 6.0 and at 50 ° C. It had a pI value of 8.6 and was stable at 55 ° C for 1 h. It hydrolyzed carboxymethylcellulose, cello-oligosaccharides (Glcn) and 4-methylumbelliferylcello-oligosaccharides but did not hydrolyze cellobiose, p-nitrophenyl β-o-glucoside, p-nitrophenyl β-d-xyloside, Avicel, filter paper and xylan. Analysis of reaction mixtures by high pressure liquid chromatography revealed that this enzyme cleaved preferentially the internal glycoside bonds of higher cello-oligosaccharides. The enzyme also catalyzed the formation of transfer products in the presence of cellotriose, cellotetraose and 4-methylumbelliferylglucoside (MeUmbGlc).
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