Purification and characterization of a thermostable lipase from newly isolated Pseudomonas sp. KWI-56.

Abstract

Newly isolated Pseudomonas sp. KWI-56 produced an extracellular thermostable lipase. The enzyme was purified 13.9-fold by acetone precipitation and gel filtration by HPLC with 2.9% recovery. The purified enzyme, which showed a single band on SDS-PAGE, had a molecular weight of 33, 000. The thermostability was very high, such that more than 96% of initial activity remained after incubation at 60°C for 24hr. The optimum temperature was 60°C and the maximum hydrolysis of beef tallow reached 95% at the reaction temperature of 50°C.