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Mode of action of a minor xylanase from Thermoascus aurantiacus on polysaccharides and model substrates
National Technical University of Athens.
National Technical University of Athens.
National Technical University of Athens.
1999 (English)In: Journal of Bioscience and Bioengineering, ISSN 1389-1723, E-ISSN 1347-4421, Vol. 87, no 6, p. 819-821Article in journal (Refereed) Published
Abstract [en]

The mode of action of a minor xylanase on a variety of polysaccharides and model substrates was investigated. The enzyme was excreted by Thermoascus aurantiacus grown in solid state fermentation (SSF). The purified enzyme had a molecular mass of 33,000. Thin layer chromatography analysis showed that the endoxylanase liberated short fragments from polysaccharides. The enzyme hydrolysed aryl-β-d-cellobioside and the chromogenic (fluorogenic) 4-methylumbelliferyl-β-glycosides of xylobiose (MeUmbXyl2) and xylotriose (MeUmbXyl3) at the agluconic linkage. The results suggested that the endoxylanase belonged to family 10.

Place, publisher, year, edition, pages
1999. Vol. 87, no 6, p. 819-821
Identifiers
URN: urn:nbn:se:ltu:diva-7074DOI: 10.1016/S1389-1723(99)80160-1Local ID: 562eeb6b-41c9-40a8-860d-78c76cf877beOAI: oai:DiVA.org:ltu-7074DiVA, id: diva2:979961
Note
Upprättat; 1999; 20130218 (ysko)Available from: 2016-09-29 Created: 2016-09-29 Last updated: 2017-11-24Bibliographically approved

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