Purification and Characterization of an Extracellular Protease from Bacillus pumilus CN8

초록

The protease produced by a Bacillus pumilus CN8 strain was purified by DEAE-Cellulose-52 ion exchange. It has a molecular weight of approximately 96,920 Dalton. In the present study, this protease showed strong activity over a broad range of pH (6.5-9.5) and temperature from 40℃ to 60℃, and the protease performed the maximal activity at pH 7.3 at 42℃. The effect of metal ions on protease activity showed that K+ could slightly increase the protease activity, and other ions such as Zn²+, Fe²+, Na+, Ca²+, Mg²+ had no significant activation or inhibition to the protease (P > 0.05), and the more important is that Cu²+, Mn²+, Sn²+, Cd²+ had a strong inhibitory effect on the protease activity.

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