Purification and Characterization of the Lipase from Marine Vibrio fischeri

Lipolytic enzymes from marine microbes have been the focus of intense and growing research. The bioluminescence bacterium Vibrio fischeri was produced lipase enzyme when the medium contained specific substrate. The lipase was purified from the concentrated culture supernatant. The most active fractions were obtained using the technique of precipitation with ammonium sulphate. The precipitated fraction was purified by desalting and ion exchange chromatography. The purified active fraction exhibiting final specific activity of 121U/mg and characterized; the optimum pH was likely between 7 to 8, the optimum temperature was 30°C and about 80 % of activity at 5°C. The enzyme was very stable at the pH 8, at the temperature 30°C. The enzyme was monomeric protein having molecular mass of 57 KDa estimated by native PAGE assay.