Cloning, expression and biochemical characterization of recombinant superoxide dismutase from Antarctic psychrophilic bacterium Pseudoalteromonas sp. ANT506
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- 作者：Quan-Fu Wang ; Yi-Fan Wang ; Yan-Hua Hou ; Yong-Lei Shi ; Han Han ; Miao Miao ; Ying-Ying Wu ; Yuan-Ping Liu ; Xiao-Na Yue and Yu-Jin Li
- 刊名：Journal of Basic Microbiology
- 出版年：2016
- 出版时间：July 2016
- 年：2016
- 卷：56
- 期：7
- 页码：753-761
- 全文大小：1190K
- ISSN：1521-4028
文摘
In this study, a superoxide dismutase gene (PsSOD) from Pseudoalteromonas sp. ANT506 was cloned and over expressed in Escherichia coli. The PsSOD has an open reading frame of 582 bp with a putative product of 193 amino acid residue and an estimated molecular size of 21.4 kDa. His-tagged PsSOD was subsequently purified 12.6-fold by Ni-affinity chromatography and the yield of 22.9%. The characterization of the purified rPsSOD exhibited maximum activity at 30 °C and pH 8.0. The enzyme exhibited 13.9% activity at 0 °C and had high-thermo lability at higher than 50 °C. rPsSOD exhibited well capability to 2.5 M NaCl (62.4%). These results indicated that rPsSOD exhibited special catalytic properties.