Purification and characterization of two xylanases from Chaetomium thermophile var. coprophile
β Scribed by Ganju, Ramesh K.; Vithayathil, Paul J.; Murthy, S. K.
- Book ID
- 120983311
- Publisher
- NRC Research Press
- Year
- 1989
- Tongue
- French
- Weight
- 1012 KB
- Volume
- 35
- Category
- Article
- ISSN
- 0008-4166
- DOI
- 10.1139/m89-140
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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,
## Abstract The ability of __Chaetomium thermophile var. coprophile__ COONEY and EMERSON to utilize carbohydrates as carbon sources for growth has been studied in stationary liquid medium at 45 Β°C. Among the monosaccharides, the highest growth was obtained on mannose, followed by xylose, glucose, a
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