KINETIC STUDIES OF PARTIALLY PURIFIED LIPASE FROM MARINE ACTINOMYCETE STREPTOMYCES ACRIMYCINI NGP 1

Abstract

This study was focused on partial purification and characterization of lipase from Streptomyces acrimyciniNGP 1, isolated from marine sediment of south Indian coastal region. In purification steps, 4.53 fold purification was achieved after 85% ammonium sulphate precipitation with 0.97 percent recovery. In further purification steps, 1.33 fold purification was achieved by Sephadex G-100 chromatography with 1.61 percent of recovery. The specific activity of purified enzyme was 1525 U/mg. Zymogram of crude enzyme on native-PAGE presented bands with lipase activity of molecular weight and Isoelectric point were 50 kDa and 7.4 respectively. These features render this lipase of interest as a biocatalyst for applications such as biodiesel production and detergent formulations.