Formation, Location, and Regulation of Endo-1,4-beta-Glucanases and beta-Glucosidases from Cellulomonas uda.

Stoppok, W; Rapp, P; Wagner, F

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.