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KMID : 0545120180280030448
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Journal of Microbiology and Biotechnology
2018 Volume.28 No. 3 p.448 ~ p.453
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Purification, Characterization, and Cloning of a Cold-Adapted Protease from Antarctic Janthinobacterium lividum
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Kim Hyun-Do
Kim Su-Mi
Choi Jong-Il
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Abstract
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In this study, a 107 kDa protease from psychrophilic Janthinobacterium lividum PAMC 26541 was purified by anion-exchange chromatography. The specific activity of the purified protease was 264 U/mg, and the overall yield was 12.5%. The J. lividum PAMC 25641 protease showed optimal activity at pH 7.0?7.5 and 40oC. Protease activity was inhibited by PMSF, but not by DTT. On the basis of the N-terminal sequence of the purified protease, the gene encoding the cold-adapted protease from J. lividum PAMC 25641 was cloned into the pET-28a(+) vector and heterologously expressed in Escherichia coli BL21(DE3) as an intracellular soluble protein.
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KEYWORD
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Cold-adapted protease, Janthinobacterium lividum, purification, expression
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