Leishmaniasis is a parasitic reticuloendotheliosis whose pathogen is a zooflagellate belonging to the genus Leishmania transmitted by the bite of an infected phlebotome. Recently, a unique secretory lipase from the human pathogen Leishmania donovani Ldlip3 has been identified and characterized. This lipase has a high identity with a putative triacylglycerol lipase of Leishmania major (Lmlip2). In the present study, Lmlip2 was expressed in the eukaryotic heterologous expression system Pichia pastoris as tagged enzyme of 308 amino acids. Maximal protein production was reached after 2 days of fermentation. Optimal Lmlip2 lipase activity was measured using the pH stat technique at pH 8 at 26 °C using vinyl esters and triacylglycerols (true lipids) as substrates. Moreover, biochemical characterization of Lmlip2 contained in culture supernatant, illustrates that L. major secreted lipase is active and stable at low temperatures especially 26°and prefer neutral pH; concerning substrate specificityLmlip2 presents a preference for short chains lipid substrates vinyl esters such as VC2, VC3 and VC4 likewise, it is capable to hydrolyze long chain triacylglycerols like olive oil. Metal ions and surfactants tested in this study decrease Lmlip2 activity. Further studies are needed to clarify the relation between the lipase activity and the virulence. Thus, it could lead to the identification of novel targets to block cutaneous Leishmaniasis in human hosts.

利什曼病是一种寄生性网状内皮病，其病原体是属于利什曼原虫属的鞭毛虫，通过被感染的抽血蚊子叮咬传播。近来，已经鉴定和表征了来自人病原体利什曼原虫多诺万尼Ldlip3的独特的分泌脂肪酶。该脂肪酶与公认的大利什曼原虫的三酰基甘油脂肪酶（Lmlip2）具有高度同一性。在本研究中，Lmlip2在真核异源表达系统巴斯德毕赤酵母中表达作为308个氨基酸的标记酶。发酵2天后达到最大蛋白质产量。使用乙烯基酯和三酰基甘油（真脂质）作为底物，使用pH stat技术在26°C下于pH 8下测量最佳Lmlip2脂肪酶活性。此外，Lmlip2的生化特性包含在培养上清，说明了硕大利什曼原虫分泌的脂肪酶在低温（尤其是26°）下具有活性且稳定，并且偏爱中性pH 关于底物的特异性Lmlip2偏爱短链脂质底物的乙烯基酯，例如VC2，VC3和VC4，它同样能够水解长链三酰基甘油，如橄榄油。在这项研究中测试的金属离子和表面活性剂会降低Lmlip2活性。需要进一步研究以阐明脂肪酶活性和毒力之间的关系。因此，它可能导致鉴定新的靶标以阻断人宿主中的皮肤利什曼病。