Purification and characterization of two cellobiohydrolases from Chaetomium thermophile var. coprophile

Ramesh, Ganju K and Murthy, SK and Paul, Vithayathil J (1989) Purification and characterization of two cellobiohydrolases from Chaetomium thermophile var. coprophile. In: Biochimica et Biophysica Acta - General Subjects, 993 (2-3). pp. 266-274.

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Abstract

Cellobiohydrolases I and II were purified to homogeneity from culture filtrates of a thermophilic fungus, Chaetomium thermophile var. coprophile, by using a combination of ion-exchange and gel filtration chromatographic procedures. The molecular weights of cellobiohydrolase I and II were estimated to be 60000 and 40000 and the enzymes were found to be glycoproteins containing 17 and 22.8% carbohydrate, respectively. The two forms differed in their amino-acid composition mainly with respect to threonine, alanine, methionine and arginine. Antibodies produced against either form of cellobiohydrolases failed to cross-react with the other. The tryptic maps of the two enzymes were found to be different. The temperature optima for cellobiohydrolase I and II were 75 and 70°C, and they were optimally active at pH 5.8 and 6.4, respectively. Both enzymes were stable at higher temperatures and were able to degrade crystalline cellulosic materals.

Item Type:	Journal Article
Publication:	Biochimica et Biophysica Acta - General Subjects
Publisher:	Elsevier Science
Additional Information:	Copyright of this article belongs to Elsevier Science.
Keywords:	Cellobiohydrolase; Enzyme purification; Enzyme characterization; (C. thermophile)
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	16 Jul 2010 09:09
Last Modified:	19 Sep 2010 06:11
URI:	http://eprints.iisc.ac.in/id/eprint/30318

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