Abstract
Thioredoxin (Trx) is a highly conserved and multi-functional protein that plays a pivotal role in maintaining the redox state of the cell and in protecting the cell against oxidative stress. Trx gene from Antarctic sea-ice bacteria Pseudoalteromonas sp. AN178 was cloned and expressed as soluble protein in Escherichia coli (designated as PsTrx). Trx gene consisted of an open reading frame of 324-bp nucleotides encoding a protein of 108 amino acids with a calculated molecular mass of 11.88kDa. The deduced protein included the conserved Cys-Gly-Pro-Cys active-site sequence. After purification by a single step Ni-NTA affinity chromatography, recombinant PsTrx with a high specific activity of 96.67U/mg was obtained. The purified PsTrx had an optimal temperature and pH of 25°C and 7.0, respectively, and showed about 55% of the residual catalytic activity even at 0-10°C. It had high tolerance to a wide range of NaCl concentrations (0-2M NaCl) and was stable in the presence of H2O2. This research suggested that PsTrx displayed unique catalytic properties.
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