LST-03 lipase from Pseudomonas aerugmosa LST-03 is highly active and stable in the presence of various organic solvents To further characterize and improve the organic solvent-stability of the LST-03 lipase, residues that potentially provide this stability were identified and mutated to other amino acids in an effort to increase the organic solvent-stability of the protein S155L, G157R, S164K, S194R, and D209N mutations were found to improve the organic solvent-stability of the wild-type LST-03 lipase Such mutations were found to Induce structural changes, including the formation of a salt bridge, hydrogen bonds, lead to an improved packing of the hydrophobic core, and pl shift of side chain These changes increased the stability of the protein, thereby improving the organic solvent-stability of the wild-type LST-03 lipase In addition, a single mutation was found to stabilize the lipase by single or multiple factors (C) 2010 Elsevier Inc All rights reserved