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Two different extracellular lipases were isolated and purified from Pseudomonas aeruginosa Ps-x to apparent homogeneity using ammonium sulfate precipitation followed by ion exchange chromatography on Q- and S-Sepharose column. Both of the purified lipases are monomeric protein with molecular weight of 15.5 and 54.97 KDa respectively. The optimal activities of the enzymes were at 45 and 50 degrees C and pHs 10.0 and 9.0. Calcium ions increase thermostability of both purified lipases I and II.pmid:16450840 fatcat:rhfmv56fwbdevmdv2axq5we454