Abstract
The genes of CS-2 lipase and its cognate foldase were cloned from Pseudomonas aeruginosa CS-2. A stop codon was not found in the lipase gene. The amino acid sequence deduced from the lipase gene from P. aeruginosa CS-2 showed 97.8%, 71.3%, and 71.2% identity with lipases from P. aeruginosa LST-03, P seudomonas mendocina ymp, and Pseudomonas stutzeri A1501, respectively. The co-expression of CS-2 lipase and its cognate foldase of P. aeruginosa CS-2 in E scherichia coli BL21 (DE3) resulted in the formation of a soluble lipase. The recombinant lipase and foldase were purified to homogeneity using nickel affinity chromatography and about 10.2-fold with 40.9% recovery was achieved for the purification of the recombinant lipase. The molecular masses of the lipase and the foldase were estimated to be 35.7 and 38.3 kDa in SDS-PAGE, respectively. The recombinant lipase showed stability in the presence of some organic solvents. The recombinant CS-2 lipase was immobilized and subsequently used for the synthesis of butyl acetate in heptane. The conversion of substrate decreased from 98.2% to 87.4% after 5 cycles in reuse of the immobilized lipase.
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The financial support from the Ministry of Science and Technology of the People’s Republic of China is gratefully acknowledged (project IDs: 2006AA020203 and 2009CB724703).
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Peng, R., Lin, J. & Wei, D. Co-Expression of an Organic Solvent-Tolerant Lipase and its Cognate Foldase of Pseudomonas aeruginosa CS-2 and the Application of the Immobilized Recombinant Lipase. Appl Biochem Biotechnol 165, 926–937 (2011). https://doi.org/10.1007/s12010-011-9309-9
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DOI: https://doi.org/10.1007/s12010-011-9309-9