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dc.contributor.authorStoppok, W
dc.contributor.authorRapp, P
dc.contributor.authorWagner, F
dc.date.accessioned2015-07-30T09:13:38Zen
dc.date.available2015-07-30T09:13:38Zen
dc.date.issued1982-07en
dc.identifier.citationFormation, Location, and Regulation of Endo-1,4-beta-Glucanases and beta-Glucosidases from Cellulomonas uda. 1982, 44 (1):44-53 Appl. Environ. Microbiol.en
dc.identifier.issn0099-2240en
dc.identifier.pmid16346067en
dc.identifier.urihttp://hdl.handle.net/10033/561226en
dc.description.abstractThe formation and location of endo-1,4-beta-glucanases and beta-glucosidases were studied in cultures of Cellulomonas uda grown on microcrystalline cellulose, carboxymethyl cellulose, printed newspaper, and some mono- or disaccharides. Endo-1,4-Glucanases were found to be extracellular, but a very small amount of cell-bound endo-1,4-beta-glucanase was considered to be the basal endoglucanase level of the cells. The formation of extracellular endo-1,4-beta-glucanases was induced by cellobiose and repressed by glucose. Extracellular endoglucanase activity was inhibited by cellobiose but not by glucose. beta-Glucosidases, on the other hand, were formed constitutively and found to be cell bound. beta-Glucosidase activity was inhibited noncompetitively by glucose. Some characteristics such as the optimal pH for and the thermostability of the endoglucanases and beta-glucosidases and the end products of cellulose degradation were determined.
dc.language.isoenen
dc.titleFormation, Location, and Regulation of Endo-1,4-beta-Glucanases and beta-Glucosidases from Cellulomonas uda.en
dc.typeArticleen
dc.contributor.departmentGesellschaft fur Biotechnologische Forschung mbH, D-38124 Braunschweig, Germany.en
dc.identifier.journalApplied and environmental microbiologyen
refterms.dateFOA2018-06-13T15:12:46Z
html.description.abstractThe formation and location of endo-1,4-beta-glucanases and beta-glucosidases were studied in cultures of Cellulomonas uda grown on microcrystalline cellulose, carboxymethyl cellulose, printed newspaper, and some mono- or disaccharides. Endo-1,4-Glucanases were found to be extracellular, but a very small amount of cell-bound endo-1,4-beta-glucanase was considered to be the basal endoglucanase level of the cells. The formation of extracellular endo-1,4-beta-glucanases was induced by cellobiose and repressed by glucose. Extracellular endoglucanase activity was inhibited by cellobiose but not by glucose. beta-Glucosidases, on the other hand, were formed constitutively and found to be cell bound. beta-Glucosidase activity was inhibited noncompetitively by glucose. Some characteristics such as the optimal pH for and the thermostability of the endoglucanases and beta-glucosidases and the end products of cellulose degradation were determined.


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