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Biochemical and cat...
Biochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Thermomyces lanuginosus ATCC 46882
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- Bennett, Neil A. (author)
- Institute of Food Research
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- Ryan, James (author)
- Institute of Food Research
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- Biely, Peter (author)
- Slovak Academy of Sciences, Bratislava
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- Vrsanska, Maria (author)
- Slovak Academy of Sciences, Bratislava
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- Kremnicky, Lubomir (author)
- Slovak Academy of Sciences, Bratislava
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- Macris, Basil J. (author)
- National Technical University of Athens
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- Kekos, Dimitris (author)
- National Technical University of Athens
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Christakopoulos, Paul (author)
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- Katapodis, Petros (author)
- National Technical University of Athens
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- Claeyssens, Marc (author)
- University of Ghent
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- Nerinckx, Wim (author)
- University of Ghent
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- Ntauma, Patricia (author)
- University of Ghent
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- Bhat, Mahalingeshwara K. (author)
- Institute of Food Research
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(creator_code:org_t)
- 1998
- 1998
- English.
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In: Carbohydrate Research. - 0008-6215 .- 1873-426X. ; 306:3, s. 445-455
- Related links:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
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- An endoxylanase (1,4-beta-D-xylan xylanohydrolase, EC 3.2.1.8) from the culture filtrates of T. lanuginosus ATCC 46882 was purified to homogeneity by DEAE-Sepharose and Bio-Gel P-30 column chromatographies. The purified endoxylanase had a specific activity of 888.8 mumol min-1 mg-1 protein and accounted for approximately 30% of the total protein secreted by this fungus. The molecular mass of native (non-denatured) and denatured endoxylanase were 26.3 and 25.7 kD as, respectively. Endoxylanase had a pI of 3.7 and was optimally active between pH 6.0-6.5 and at 75 degrees C. The enzyme showed > 50% of its original activity between pH 5.5-9.0 and at 85 degrees C. The pH and temperature stability studies revealed that this endoxylanase was almost completely stable between pH 5.0-9.0 and up to 60 degrees C for 5 h and at pH 10.0 up to 55 degrees C for 5 h. Thin-layer chromatography (TLC) analysis showed that endoxylanase released mainly xylose (Xyl) and xylobiose (Xyl2) from beechwood 4-O-methyl-D-glucuronoxylan, O-acetyl-4-O-methyl-D-glucuronoxylan and rhodymenan (a beta-(1-->3)-beta(1-->4)-xylan). Also, the enzyme released an acidic xylo-oligosaccharide from 4-O-methyl-D-glucuronoxylan, and an isomeric xylotetraose and an isomeric xylopentaose from rhodymenan. The enzyme hydrolysed [1-3H]-xylo-oligosaccharides in an endofashion, but the hydrolysis of [1-3H]-xylotriose appeared to proceed via transglycosylation. since the xylobiose was the predominant product. Endoxylanase was not active on pNPX and pNPC at 40 and 100 mM for up to 6 h, but showed some activity toward pNPX at 100 mM after 20-24 h. The results suggested that the endoxylanase from T. lanuginosus belongs to family 11.
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- By the author/editor
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Bennett, Neil A.
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Ryan, James
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Biely, Peter
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Vrsanska, Maria
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Kremnicky, Lubom ...
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Macris, Basil J.
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show more...
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Kekos, Dimitris
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Christakopoulos, ...
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Katapodis, Petro ...
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Claeyssens, Marc
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Nerinckx, Wim
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Ntauma, Patricia
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Bhat, Mahalinges ...
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- Articles in the publication
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Carbohydrate Res ...
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Luleå University of Technology