Purification and Some Properties of Lipase Produced by Pseudomonas fragi22.39 B

Abstract

The lipase (EC. 3.1.1.3) of Pseudomonas fragi 22.39 B was purified by acidification of the culture supernatant, ammonium sulfate fractionation, and column chromatography on DEAE- Toyopearl 650 m and DEAE-Sepharose CL-6B. The recovery of activity was about 48%. The purified lipase was homogeneous electrophoretically and its molecular weight was 33,000. The optimum pH and temperature for hydrolysis of olive oil emulsion were 9.0 and 65°C, respectively. The enzyme was stable up to 51°C at pH 9.0 for 24 hr and in a pH range from 6.5 to 10.5 at 30°C for 24 hr. The lipase was inhibited by Zn^{2 +}, Fe^{2 +}, Fe^{3 +} and cationic surfactants such as cetyltrimethyl- ammonium bromide.