Formation, Location, and Regulation of Endo-1,4-beta-Glucanases and beta-Glucosidases from Cellulomonas uda.
| dc.contributor.author | Stoppok, W | |
| dc.contributor.author | Rapp, P | |
| dc.contributor.author | Wagner, F | |
| dc.date.accessioned | 2015-07-30T09:13:38Z | en |
| dc.date.available | 2015-07-30T09:13:38Z | en |
| dc.date.issued | 1982-07 | en |
| dc.identifier.citation | Formation, 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.issn | 0099-2240 | en |
| dc.identifier.pmid | 16346067 | en |
| dc.identifier.uri | http://hdl.handle.net/10033/561226 | en |
| dc.description.abstract | The 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.iso | en | en |
| dc.title | Formation, Location, and Regulation of Endo-1,4-beta-Glucanases and beta-Glucosidases from Cellulomonas uda. | en |
| dc.type | Article | en |
| dc.contributor.department | Gesellschaft fur Biotechnologische Forschung mbH, D-38124 Braunschweig, Germany. | en |
| dc.identifier.journal | Applied and environmental microbiology | en |
| refterms.dateFOA | 2018-06-13T15:12:46Z | |
| html.description.abstract | The 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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