Bacterial esterases are highly versatile enzymes, currently widely used in detergents, biosurfactants, bioemulsifiers and as biocatalysts in paper and food industries. Present work describes heterologous expression, purification, and biophysical and biochemical characterization of a halotolerant esterase from Bacillus licheniformis (BlEstA). BlEstA preferentially cleaves pNP-octanoate and both activity and stability of the enzyme increased in the presence of 2 M NaCl, and also with several organic solvents (ethanol, methanol and DMSO). Furthermore, BlEstA has considerable emulsifying properties, particularly with olive oil as substrate. Our studies also show that the enzyme is monomeric in solution and its small-angle X-ray scattering low-resolution molecular envelope fits well its high-resolution homology model.

细菌酯酶是高度通用的酶，目前广泛用于洗涤剂，生物表面活性剂，生物乳化剂以及造纸和食品工业中的生物催化剂。目前的工作描述了地衣芽孢杆菌（Bl EstA）的卤代烷酯酶的异源表达，纯化以及生物物理和生物化学表征。BL ESTA优先切割的pNP -octanoate和酶的活性和稳定性在2M NaCl的存在下，用几种有机溶剂（乙醇，甲醇和DMSO）增加，也。此外，BlEstA具有相当大的乳化性能，尤其是以橄榄油为底物。我们的研究还表明，该酶在溶液中为单体，其小角X射线散射低分辨率分子包膜非常适合其高分辨率同源性模型。