characterization of a lipase from a newly isolated pseudomonas sp.

background and objectives: lipases are valuable biocatalysts which are widely used in the detergent, food, dairy and pharmaceutical industries. the aims of the present study included the isolation of a lipase-producer from industrial zones and the partial characterization of the enzyme. materials and methods: a number of bacteria were isolated from sites related to the oil industries. an isolate forming a halo zone in a selective medium (tw agar) was then selected and grown on a medium suitable for the production of lipase. the isolate was subsequently identified by the 16s rrna sequencing method, and its enzyme activity was measured by a spectrophotometer using p npp as a substrate. results: the selected isolate was identified by the molecular method as pseudomonas sp. its extracellular lipase activity was 41.5 ± 1.4 u/ml, and the high affinity of this enzyme for the substrate was indicated by the kinetic parameters of km and vm, which were estimated by the the lineweaver-burk plot as 0.77 mm and 49.5 u/ml, respectively. activation energy of lipase calculated from the arrhenius plot was found to be 20.78 kj/mol, and a temperature coefficient (q10) of 4.39 indicated the high catalytic activity of the enzyme and the temperature dependence of the enzymatic reaction. conclusion: the results demonstrated that the indigenous isolate could have potential applications in many relevant industries.