Abstract
This study reported the cloning, expression, and characterization of a new salt-tolerant leucine dehydrogenase (PrLeuDH) from Pseudoalteromonas rubra DSM 6842. A codon-optimized 1038bp gene encoding PrLeuDH was successfully expressed on pET-22b( +) in E. coli BL21(DE3). The purified recombinant PrLeuDH showed a single band of about 38.7kDa on SDS-PAGE. It exhibited the maximum activity at 40°C and pH 10.5, while kept high activities in the range of 25-45°C and pH 9.5-12. The Km value and turnover number kcat for leucine of PrLeuDH were 2.23 ± 0.12mM and 35.39 ± 0.05s-1, respectively, resulting in a catalytic efficiency kcat/Km of 15.87s-1/mM. Importantly, PrLeuDH remained 92.1 ± 2.67% active in the presence of 4.0M NaCl. The study provides the first in-depth understanding of LeuDH from marine Pseudoalteromonas rubra, meanwhile the unique properties of high activity at low temperature and high salt tolerance make it a promising biocatalyst for the synthesis of non-protein amino acids and α-ketoacids under special conditions in pharmaceutical industry.
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