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Characterization of cellulolytic enzyme component from Aspergillus terreus and its mutant

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dc.contributor.author Araujo, A.
dc.contributor.author D'Souza, J.
dc.date.accessioned 2015-06-02T09:52:31Z
dc.date.available 2015-06-02T09:52:31Z
dc.date.issued 1986
dc.identifier.citation Journal of Fermentation Technology. 64(5); 1986; 463-467. en_US
dc.identifier.uri http://dx.doi.org/10.1016/0385-6380(86)90037-3
dc.identifier.uri http://irgu.unigoa.ac.in/drs/handle/unigoa/65
dc.description.abstract Cellulases produced by Aspergillus terreus ATCC 52430 and its mutant, UNGI-40,were resolved into four components, one beta-glucosidase , an exoglucanase, and two endoglucanases (Endo I and II) by gel filtration and ion-exchange chromatography on DEAE-Sephadex. The homogeneity of the components was checked on polyacrylamide gels. These components act synergistically and are required to break down insoluble cellulose completely; this was studied by mixing various components. The enzymes had variations in activities at different pHs and temperatures. The optimum pH and temperature for all the components are reported. There was also variations in their carbohydrate content. THe molecular weight or cellulases from A. terreus ATCC 52430 were beta-glucosidase 90,000; exoglucanase 70,000; endoglucanase I 78,000; and 16,000 for endoglucanase II; but the mutant beta-glucosidase was 95,000; exoglucanase 68,000; and 78,000 and, 26,000 for endoglucanases I and II, respectively. en_US
dc.publisher Elsevier en_US
dc.subject Microbiology en_US
dc.title Characterization of cellulolytic enzyme component from Aspergillus terreus and its mutant en_US
dc.type Journal article en_US


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