Purification and Characterization of the Lipase from Marine Vibrio fischeri

Abstract

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