TY - JOUR AB - An organic solvent-tolerant lipase from newly isolated Pseudomonas aeruginosa LX1 has been purified by ammonium sulfate precipitation and ion-exchange chromatography leading to 4.3-fold purification and 41.1% recovery. The purified lipase from P. aeruginosa LX1 was homogeneous as determined by SDS-PAGE, and the molecular mass was estimated to be 56 kDa. The optimum pH and temperature for lipase activity were found to be 7.0 and 40 degrees C, respectively. The lipase was stable in the pH range 4.5-12.0 and at temperatures below 50 degrees C. Its hydrolytic activity was found to be highest towards p-nitrophenyl palmitate (C16) among the various p-nitrophenol esters investigated. The lipase displayed higher stability in the presence of various organic solvents, such as n-hexadecane, isooctane, n-hexane, DMSO, and DMF, than in the absence of an organic solvent. The immobilized lipase was more stable in the presence of n-hexadecane, tert-butanol, and acetonitrile. The transesterification activity of the lipase from P. aeruginosa LX1 indicated that it is a potential biocatalyst for biodiesel production. (C) 2010 Elsevier B.V. All rights reserved. AD - He, BF AN - WOS:000281321100003 AU - Ji, Q. C. AU - Xiao, S. J. AU - He, B. F. AU - Liu, X. N. DA - Oct DO - 10.1016/j.molcatb.2010.06.001 IS - 3-4 J2 - J Mol Catal B-Enzym KW - pseudomonas aeruginosa LA - English N1 - 643td PY - 2010 SN - 1381-1177 SP - 264-269 ST - Purification and characterization of an organic solvent-tolerant lipase from Pseudomonas aeruginosa LX1 and its application for biodiesel production T2 - Journal of Molecular Catalysis B-Enzymatic TI - Purification and characterization of an organic solvent-tolerant lipase from Pseudomonas aeruginosa LX1 and its application for biodiesel production UR - http://www.sciencedirect.com/science/article/pii/S1381117710001426 VL - 66 ID - 2608 ER -