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Purification and characterization of two low molecular mass alkaline xylanases from Fusarium oxysporum F3
University of Ghent.
National Technical University of Athens.
National Technical University of Athens.
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1996 (English)In: Journal of Biotechnology, ISSN 0168-1656, E-ISSN 1873-4863, Vol. 51, no 2, p. 181-189Article in journal (Refereed) Published
Abstract [en]

Two low molecular mass endo-1,4-β-d-xylanases from Fusarium oxysporum were purified to homogeneity by gel-filtration and ion-exchange chromatography. They exhibit molecular masses of 20.8 (xylanase I) and 23.5 (xylanase II) kDa, and isoelectric points of 9.5 and 8.45–8.70, respectively. Both xylanases display remarkable pH (9.0) stability. At 40 to 55 °C xylanase II is more thermostable than xylanase I but less active on xylan. In contrast to xylanase I, xylanase II is able to hydrolyze 1-O-4-methylumbelliferyl-(β-d-glucopyranosyl)-β-d-xylopyranoside (muxg). Neither of these enzymes hydrolyze xylotriose. They bind on crystalline cellulose but not on insoluble xylan. Analysis of reaction mixtures by high pressure liquid chromatography revealed that both enzymes cleave preferentially the internal glycosidic bonds of xylopentaose and oat spelts xylan. Thus the purified enzymes appeared to be true endo-β-1,4-xylanases. The amino terminal sequences of xylanases I and II show no homology. Xylanase I shows high similarity with alkaline low molecular mass xylanases of family G/11.

Place, publisher, year, edition, pages
1996. Vol. 51, no 2, p. 181-189
Identifiers
URN: urn:nbn:se:ltu:diva-4257DOI: 10.1016/0168-1656(96)01619-7Local ID: 22e7a81f-025b-4cd9-ad9a-df438098e480OAI: oai:DiVA.org:ltu-4257DiVA: diva2:977121
Note
Upprättat; 1996; 20130219 (ysko)Available from: 2016-09-29 Created: 2016-09-29 Last updated: 2017-11-24Bibliographically approved

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