Purification and functional characteristics of an endocellulase from Chaetomium thermophile var. coprophile

Ganju, Ramesh K and Murthy, SK and Vithayathil, Paul J (1990) Purification and functional characteristics of an endocellulase from Chaetomium thermophile var. coprophile. In: Carbohydrate Research, 197 . pp. 245-255.

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Abstract

An endocellulase (1→4)-β-d-glucan 4-glucanohydrolase was isolated from the culture filtrates of Chaetomium thermophile. The enzyme was homogeneous by PAGE and SDS-PAGE. The molecular weight was 36 000 by SDS-PAGE and 38 000 by gel filtration. It was a glycoprotein. From the amino acid composition, it was found to be rich in glycine, threonine, and aspartic and glutamic acids, but contained only low proportions of histidine and sulfur-containing amino acids. It was optimally active at pH 6 and at 60°. The enzyme did not hydrolyze cellobiose and cellotriose, but hydrolyzed cello-tetraose, -pentaose, and -hexaose at comparable rates. It was specific for molecules containing β-(1→4) linkages. It showed high activity towards amorphous cellulose, and the reaction products contained cellobiose to cellopentaose, showing that it effects random cleavage of cellulose.

Item Type:	Journal Article
Publication:	Carbohydrate Research
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Science.
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	12 Jan 2011 11:13
Last Modified:	12 Jan 2011 11:13
URI:	http://eprints.iisc.ac.in/id/eprint/34975

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