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- Title
Cloning, expression and biochemical characterization of recombinant superoxide dismutase from Antarctic psychrophilic bacterium Pseudoalteromonas sp. ANT506.
- Authors
Wang, Quan‐Fu; Wang, Yi‐Fan; Hou, Yan‐Hua; Shi, Yong‐Lei; Han, Han; Miao, Miao; Wu, Ying‐Ying; Liu, Yuan‐Ping; Yue, Xiao‐Na; Li, Yu‐Jin
- Abstract
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. Histagged 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 2.5M NaCl (62.4%). These results indicated that rPsSOD exhibited special catalytic properties.
- Subjects
SUPEROXIDE dismutase; PSYCHROPHILIC bacteria; GENE expression in bacteria; ESCHERICHIA coli; AMINO acids; CHROMATOGRAPHIC analysis
- Publication
Journal of Basic Microbiology, 2016, Vol 56, Issue 7, p753
- ISSN
0233-111X
- Publication type
Article
- DOI
10.1002/jobm.201500444