Purification and Characterization of an Extracellular Protease from Bacillus pumilus CN8
Mei Hu, Yong Guo Jin, Hao Li Li, Jun Wang, Hana Kim, Deog Hwan Oh
Abstract
Mei Hu, Yong Guo Jin, Hao Li Li, Jun Wang, Hana Kim, Deog Hwan Oh
Abstract
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 40oC to 60oC, and the protease performed the maximal activity at pH 7.3 at 42oC. 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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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 40oC to 60oC, and the protease performed the maximal activity at pH 7.3 at 42oC. 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.
Key concepts: Protease, Bacillus pumilus, Chemistry, Extracellular, Biochemistry, Enzyme, Chromatography, Bacteria