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Purification and characterization of two xylanases from Chaetomium thermophile var. coprophile

Ganju, Ramesh K and Vithayathil, Paul J and Murthy, SK (1989) Purification and characterization of two xylanases from Chaetomium thermophile var. coprophile. In: Canadian Journal of Microbiology, 35 (9). pp. 836-842.

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Two xylanases (I and II) out of several extracellular xylanases produced by the thermophilic fungus Chaetomium thermophile var. coprophile were purified to homogeneity by a combination of ion exchange and gel filtration chromatographic procedures. They had molecular weights of 26 000 (xylanase I) and 7000 (xylanase II). The temperature optima for xylanase I and II were 70 and 60 °C, and they were optimally active at pH 4.8–6.4 and 5.4–6.0, respectively. Xylanase I was found to be comparatively more stable than xylanase II at higher temperatures. Amino acid composition indicated that xylanase I contained high amounts of glycine, threonine, and low amounts of histidine and sulphur-containing amino acids. Each enzyme released different hydrolysis products from larch wood xylan. Xylanase I produced mainly xylobiose and xylotriose whereas xylanase II produced mainly xylobiose

Item Type: Journal Article
Publication: Canadian Journal of Microbiology
Publisher: NRC Research Press
Additional Information: Copyright of this article belongs to NRC Research Press.
Keywords: Xylanase;enzyme purification;characterization;Chaetomium thermophile
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 28 Dec 2007
Last Modified: 27 Aug 2008 13:08
URI: http://eprints.iisc.ac.in/id/eprint/12808

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