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- W1963972235 abstract "Conditions for the production of extracellular carboxymethyl cellulase (CMCase) and avicelase activities by a locally isolated Cellulomonas species identified as C. flavigena were optimized. The microbe produced maximal levels of free cellulases after 72 h of fermentation, when cultivated in the presence of 0.2% yeast extract, 0.5% Avicel, and 0.1% Tween 80 at 30°C. Conditions for the elution of substrate-bound cellulases from the residual Avicel were optimized. Higher proportions of the extracellular cellulases were bound to the substrate when higher concentrations of Avicel were used. When 2.0% Avicel was used as a carbon source, maximal levels of extracellular CMCase and avicelase produced were 13.2 and 3 U ml−1of the culture medium, respectively. Both the cellulases were most active at pH 6.5 and 50°C and were inhibited by β-mercaptoethanol. Calcium chloride activated CMCase but had no effect on avicelase activity. Each of the enzymes lost activity when incubated at 70°C for 30 min. A comparative study of free and substrate-bound CMCase on gradient polyacrylamide gel electrophoresis (PAGE) showed that free CMCase activity was composed of at least seven active fractions, while bound activity had four major bands of CMCase activity. Since a considerable level of protease was secreted by C. flavigena, the additional fractions in the free CMCase activity could be a result of proteolysis." @default.
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- W1963972235 date "1988-10-01" @default.
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- W1963972235 title "Production of free and substrate-bound cellulases of Cellulomonas flavigena" @default.
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- W1963972235 doi "https://doi.org/10.1016/0141-0229(88)90110-x" @default.
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