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KMID : 0881720110260010076
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Journal of Food Hygiene and Safety
2011 Volume.26 No. 1 p.76 ~ p.81
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Purification and Characterization of an Extracellular Protease from Bacillus pumilus CN8
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Jin Yong-Guo
Li Hao-Li
Ma Mei-Hu
Jun Wang
Kim Ha-Na
Oh Deog-Hwan
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Abstract
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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.
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KEYWORD
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Bacillus pumilus, Protease, Purification, Characterization
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