PURIFICATION AND CHARACTERIZATION OF A THERMOSTABLE LIPASE FROM NEWLY ISOLATED PSEUDOMONAS SP KWI-56

Newly isolated Pseudomonas sp. KWI-56 produced an extracellular thermostable lipase. The enzyme was purified 13.9-fold by acetone precipitation and gel nitration 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 24 hr. The optimum temperature was 60°C and the maximum hydrolysis of beef tallow reached 95% at the reaction temperature of 50°C. © 1990 by the Japan Society for Bioscience, Biotechnology, and Agrochemistry. All rights reserved.