Article Abstract:
The cloning and sequencing of the lipase gene (lipP) from a Pseudomonas strain and the purification and characterization of the recombinant enzyme LipP were studied and reported. The amino acid sequence from the nucleotide sequence of the gene corresponded to a protein of 308 amino acid residues with a molecular weight of 33,714. The LipP enzyme was found to be stable between pH 6 and 9 while ts was unstable with temperatures higher than 45 degrees C. Various organic solvents such as dimethyl sulfoxide and methanol at concentrations of 0 to 30% activated the enzyme.
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Article Abstract:
Research was conducted to examine the characteristics of a cold-active recombinant subtilisinlike protease from the psychrotrophic bacterium Shewanella strain Ac10. The amino acid sequence deduced from the 2,442-bp nucleotide sequence showed that the protein was 814 amino acids long with an estimated molecular weight of 85,113. Purification was performed from the culture supernatant of Escherichia coli recombinant cells using affinity chromatography with a bacitracin-Sepharose column.
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Article Abstract:
A low-temperature protein expression system was constructed using an Antarctic cold-adapted bacterium Shewanella sp. strain Ac10, as the host. The maximum yield of proteins was obtained when the promoter for putative alkyl hydroperoxide reductase (ahpC) was used and the recombinant cells were grown to late stationary phase.
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