Cloning, expression and biochemical characterization of recombinant superoxide dismutase from Antarctic psychrophilic bacterium Pseudoalteromonas sp. ANT506
In this study, a superoxide dismutase gene ( Ps SOD) from Pseudoalteromonas sp. ANT506 was cloned and over expressed in Escherichia coli . The Ps SOD 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 Ps SOD w...
Published in: | Journal of Basic Microbiology |
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Main Authors: | , , , , , , , , , |
Other Authors: | , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Wiley
2015
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Subjects: | |
Online Access: | http://dx.doi.org/10.1002/jobm.201500444 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fjobm.201500444 https://onlinelibrary.wiley.com/doi/pdf/10.1002/jobm.201500444 |
Summary: | In this study, a superoxide dismutase gene ( Ps SOD) from Pseudoalteromonas sp. ANT506 was cloned and over expressed in Escherichia coli . The Ps SOD 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 Ps SOD was subsequently purified 12.6‐fold by Ni‐affinity chromatography and the yield of 22.9%. The characterization of the purified r Ps SOD 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. r Ps SOD exhibited well capability to 2.5 M NaCl (62.4%). These results indicated that r Ps SOD exhibited special catalytic properties. |
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