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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