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...

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Bibliographic Details
Published in:Journal of Basic Microbiology
Main 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
Other Authors: National Natural Science Foundation of China, Natural Science Foundation of Shandong Province
Format: Article in Journal/Newspaper
Language:English
Published: Wiley 2015
Subjects:
Applied Microbiology and Biotechnology
General Medicine
Antarctic
Antarc*
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
Description
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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