Lipase is of great interest to the pharmaceutical and food industry; furthermore it could be used in the obtention process of biodiesel. The recombinant enzyme will make possible the obtention of larger lipase quantities with a lower cost, optimizing the productive process. Therefore, the aim of this work was to clone a Staphylococcus warneri EX17 lipase, study its expression and activity in different cultivation conditions in Escherichia coli. Four strains (BL21 (DE3), C43 (DE3), Rosetta (DE3), and Rosetta-gami 2 (DE3)) were studied in LB and TB growth medium, at 30°C and 37°C. The cells were induced with 1 mM IPTG (Isopropyl β-D-1-thiogalactopyranoside) at an optical density of 0.4-0.6 at 600 nm. For all strains, the better expression condition was achieved with LB medium at 30°C. The highest enzymatic activity obtained was in the soluble fraction of BL21(DE3) strain, after 9 hours induction, showing a specific activity of 0.046 U/mg when using LB medium at 30°C.