Purification and functional characteristics of an endocellulase from Chaetomium thermophile var. coprophile
Data(s) |
25/03/1990
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Resumo |
An endocellulase (1→4)-β-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 β-(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. |
Formato |
application/pdf |
Identificador |
http://eprints.iisc.ernet.in/34975/1/Endo.pdf Ganju, Ramesh K and Murthy, SK and Vithayathil, Paul J (1990) Purification and functional characteristics of an endocellulase from Chaetomium thermophile var. coprophile. In: Carbohydrate Research, 197 . pp. 245-255. |
Publicador |
Elsevier Science |
Relação |
http://dx.doi.org/10.1016/0008-6215(90)84147-M http://eprints.iisc.ernet.in/34975/ |
Palavras-Chave | #Biochemistry |
Tipo |
Journal Article PeerReviewed |