Purification and characterization of endo-1,4-β-xylanase from Paecilomyces varioti Bainier

Krishnamurthy, Savita and Vithayathil, Paul Joseph (1989) Purification and characterization of endo-1,4-β-xylanase from Paecilomyces varioti Bainier. In: Journal of Fermentation and Bioengineering, 67 (2). pp. 77-82.

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Abstract

An endo-xylanase (1,4-β-d-xylanxylanohydrolase EC 3.2.1.8) was isolated from the culture filtrate of Paecilomyces varioti Bainier. The enzyme was purified 3.2 fold with a 60% yield by gel filtration and ion exchange chromatography. The purified enzyme had a molecular weight of 25,000 with a sedimentation coefficient of 2.2 S. The isoelectric point of the enzyme was 3.9. The enzyme was obtained in crystalline form. The optimum pH range was 5.5–7.0 and the temperature, 65°C. The Michaelis constant was 2.5 mg larchwood xylan/ml. The enzyme was found to degrade xylan by an endo mechanism producing arabinose, xylobiose, xylo- and arabinosylxylo-oligosaccharides, during the initial stages of hydrolysis. On prolonged incubation, xylotriose, arabinosylxylotriose and xylobiose were the major products with traces of xylotetraose, xylose and arabinose.

Item Type:	Journal Article
Publication:	Journal of Fermentation and Bioengineering
Publisher:	Elsevier science
Additional Information:	Copyright of this article belongs to Elsevier science.
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	26 Aug 2010 07:58
Last Modified:	19 Sep 2010 06:14
URI:	http://eprints.iisc.ac.in/id/eprint/31539

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