Purification and characterization of lipase from psychrophilic Acinetobacter calcoaceticus LP009

Abstract

A lipase-producing bacterium, Acinetobacter calcoacetius LP009, was isolated from raw milk. The optimum conditions for growth and lipase production by A. calcoaceticus LP009 were 15 °C with shaking at 200 rpm in LB supplemented with 1.0% (v/v) Tween 80. The crude lipase was purified to homogeneous state by ultrafiltration and gel filtration chromatography on Sephadex G-100. Its molecular weight determined by SDS-PAGE was 23 kDa and it exhibited maximum activity at pH 7.0 and 50°C. It was stable over the pH range of 4.0 to 8.0 and at temperatures lower than 45 °C. It was a metallo-enzyme that is positionally non-specific and had the ability to improve fat hydrolysis in soybean meal and in premixed animals feed.