title: Purification and characterization of two cellobiohydrolases from Chaetomium thermophile var. coprophile.
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 60,000 and 40,000 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 degrees 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 materials.
authors.affiliation: Department of Biochemistry, Indian Institute of Science, Bangalore.
authors.forename: R K
authors.initials: RK
authors.lastname: Ganju
authors.forename: S K
authors.initials: SK
authors.lastname: Murthy
authors.forename: P J
authors.initials: PJ
authors.lastname: Vithayathil
mesh_terms: D000596:Amino Acids / Q000032:analysis; D001203:Ascomycota / Q000201:enzymology*; D002482:Cellulose / Q000378:metabolism; D043366:Cellulose 1,4-beta-Cellobiosidase; D002597:Chaetomium / Q000201:enzymology*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D006026:Glycoside Hydrolases / Q000032:analysis / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D013696:Temperature
chemical_list: D000596:Amino Acids; D010446:Peptide Fragments; D002482:Cellulose; D006026:Glycoside Hydrolases; D043366:Cellulose 1,4-beta-Cellobiosidase