Purification and functional characteristics of an endocellulase from Chaetomium thermophile var. coprophile
✍ Scribed by Ramesh K. Ganju; S.K. Murthy; Paul J. Vithayathil
- Publisher
- Elsevier Science
- Year
- 1990
- Tongue
- English
- Weight
- 728 KB
- Volume
- 197
- Category
- Article
- ISSN
- 0008-6215
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✦ Synopsis
An endocellulase (1-34)~P-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 p-(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.