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
School of Marine and Technology, Harbin Institute of Technology, Weihai, P.R. China.
Shandong Provincial Engineering Technology Research Center of Marine Health Food, Rongcheng, P.R. China.
J Basic Microbiol. 2016 Jul;56(7):753-61. doi: 10.1002/jobm.201500444. Epub 2015 Sep 30.
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.
在本研究中，克隆了来自假交替单胞菌ANT506的超氧化物歧化酶基因（PsSOD），并在大肠杆菌中进行了过量表达。PsSOD的开放阅读框为582 bp，推测产物为193个氨基酸残基，估计分子大小为21.4 kDa。随后，His标签的PsSOD通过镍亲和层析纯化了12.6倍，产率为22.9%。纯化的rPsSOD的特性表明其在30°C和pH 8.0时具有最大活性。该酶在0°C时具有13.9%的活性，在高于50°C时具有高热稳定性。rPsSOD对2.5 M NaCl表现出良好的耐受性（62.4%）。这些结果表明rPsSOD具有特殊的催化特性。
