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• W2561353998 abstract "Broth incubated with Bacillus subtilis YJ1 at 37°C for 36 h was collected and removed bacterial cells by passing through a 0.45 µm membrane. A cellulase was purified to electrophoretical homogeneity by ammonium sulfate precipitation, Macro-Prep ion exchange and Bio-Gel P-100 chromatography. The recovery and purification fold were 9.7% and 289, respectively, after Bio-Gel P-100 chromatograph. The purified cellulase, with a molecular mass (M) of 32.5 kDa, had an optimal pH and temperature at 6.0 and 50-60°C, respectively. It was stable at pH 6.0-7.5 and <50°C. The purified cellulase was activated by Mn 2+ and Co 2+ , but inhibited by SDS, p-CMB, DTT, Hg + , Cd 2+ , Fe 2+ and Fe 3+ . According to substrate specificity, the purified cellulase has high specificity to CMC and was considered to be an endo-1,4-glucanase." @default.
• W2561353998 created "2017-01-06" @default.
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• W2561353998 date "2010-06-15" @default.
• W2561353998 modified "2023-10-18" @default.
• W2561353998 title "PURIFICATION AND CHARACTERIZATION OF A CELLULASE FROM BACILLUS SUBTILIS YJ1" @default.
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• W2561353998 doi "https://doi.org/10.51400/2709-6998.1895" @default.
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