Applied and Environmental Microbiology · 1982 · 90 citations · 36 references
Life SciencesBiochemistryMicrobiologyCarbohydrate BiochemistryEnzymologyMicrobial PhysiologyCellulose BiochemistryGlycan DegradationBeta-glucan DegradationBeta-glucosidase ActivityCellulase EnzymesCellulose BreakdownCellulose DegradationFermentation End ProductsOptimal Ph Determinationβ-Glucosidase Activity
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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