本研究由伯克霍爾德氏菌(Burkholderia sp.)中選殖出一組脂肪酶基因(lp)及其伴護子基因(lpc)，分別以不同的表現載體於大腸桿菌中中進行異源蛋白之共表現，將純化透析後的重組蛋白進行活性分析，發現此脂肪酶需要伴護子蛋白的協助才具有活性，且脂肪酶上的訊息胜肽存在與否也對活性造成影響。經由脂肪酶的特性分析得知，此酵素為偏鹼性脂肪酶、耐熱性佳，以4-硝基苯酯為基質進行水解反應時，具有廣泛的基質特異性，在不同的溫度下也都有很好的水解反應，尤其此酵素具有很好的轉酯化能力可應用於健康油脂生產。

Both lipase gene (lp) and lipase-specific chaperone gene (lpc) of Burkholderia sp. were cloned into different expression 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 lipasespecific 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.