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Cloning, expression and biochemical characterization of recombinant superoxide dismutase from Antarctic psychrophilic bacterium Pseudoalteromonas sp. ANT506
Author(s) -
Wang QuanFu,
Wang YiFan,
Hou YanHua,
Shi YongLei,
Han Han,
Miao Miao,
Wu YingYing,
Liu YuanPing,
Yue XiaoNa,
Li YuJin
Publication year - 2016
Publication title -
journal of basic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0233-111X
DOI - 10.1002/jobm.201500444
Subject(s) - psychrophile , recombinant dna , cloning (programming) , bacteria , microbiology and biotechnology , superoxide dismutase , pseudoalteromonas , biology , biochemistry , molecular cloning , enzyme , chemistry , gene , gene expression , 16s ribosomal rna , genetics , computer science , programming language
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.