Both lipase gene (lp) and lipase-specific chaperone gene (lpc) of Burkholderia sp. were cloned into different express ion vectors and co-expressed in heterologous host Escherichia coli. After purification and dialysis, the enzymatic activity of the recombinant protein was analyzed. The results showed that the lipase-specific chaperone was required for the lipase activity and the signal peptide of the lipase played an important role in the lipase activity. In addition, the recombinant enzyme was an alkaline lipase with a broad range of 4-nitrophenyl ester substrates and thermo-stability. Furthermore, the recombinant lipase had excellent capability for trans-esterification in oil production.