The present study was aimed to express in Escherichia coli of an extracellular lipase from a local soil isolate. The lipase gene from soil isolate bacillus subtilis strain was cloned previously. The cloned gene in pTZ57R was digested out using NdeI and BamHI restriction enzymes. The extracted insert was ligated into pET15b expression vector and transformed in E. coli BL21 (DE3). The expression of the recombinant lipase was induced using 1 mM IPTG. Cells were harvested after 3 hours of induction and resuspended in a lysis solution containing 8 M urea and 20 mM Tris-HCl pH 8. Crude cell extract was used to determine enzyme activity after dialysis. The enzyme activity was measured by spectrophotometry at 400 nm using p-nitrophenyl-decanoate as a substrate. The recombinant lipase showed a molecular weight of approximately 25 kDa by SDS-PAGE. Maximum activity was found at pH 9-10 and 40-50 • C. The recombinant lipase also showed remarkable activity in a range of pH values from 6-11 and in a temperature range of 30-80 • C. ZnCl 2 concentrations including 1 mM, 0.3 mM, 0.1 mM, 0.03 mM, and 0.01 mM were examined for their effect on enzyme activity and thermostability. The results showed that ZnCl 2 at all concentrations were inhibitory to the enzyme activity and did not improve enzyme thermostability. In conclusion, the recombinant lipase showed better activity with respect to temperature as compared to lipase LipA from bacillus subtilis (its closest relative in primary structure) while their activities were similar in the alkaline pH.