A glutathione peroxidase from Antarctic psychrotrophic bacterium Pseudoalteromonas sp ANT506: Cloning and heterologous expression of the gene and characterization of recombinant enzyme

作者：Wang, Yatong; Han, Han; Cui, Bingqing; Hou, Yanhua^*; Wang, Yifan; Wang, Quanfu^*

来源：Bioengineered, 2017, 8(6): 742-749.

DOI：10.1080/21655979.2017.1373534

• glutathione peroxidase
• expression
• psychrotrophic
• Antarctic sea ice
• gene

A glutathione peroxidase (GPx) gene, designated as PsGPx, was cloned from Antarctic psychrotrophic bacterium Pseudoalteromonas sp. ANT506 and expressed in Escherichia coli. The full-length PsGPx contained a 585-bp encoding 194 amino acids with predicted molecular masses of approx. 21.7 kDa. Multiple sequence alignments revealed that PsGPx belonged to the thioredoxin- like superfamily. PsGPx was heterologously overexpressed in E. coli, purified and characterized. The maximum catalytic temperature and pH value for recombinant PsGPx (rPsGPx) were 30 degrees C and pH 9.0, respectively. rPsGPx retained 45% of the maximum activity at 0 degrees C and exhibited high thermolability with a half-life of approx. 40 min at 40 degrees C. In addition, the enzymatic activity of rPsGPx was still manifested under 3 M NaCl. The Km and Vmax values of the recombinant enzyme using GSH and H2O2 as substrates were 1.73 mM and 16.28 nmol/mL/min versus 2.46 mM and 21.50 nmol/mL/min, respectively.

• 出版日期2017
• 单位哈尔滨工业大学