Purification and Characterization of Lipase Enzyme from Poppy Seed (Papaver somniferum L.)

Lipases are enzymes which provide the hydrolysis of triglycerides. With the technological progress the use of lipases is increased and the lipase isolation and purification got more important. Therefore purification studies are increased also. In this study it was aimed to purify and characterize the lipase enzyme from poppy seed. It is received lipase from poppy seed for the first time. Lipase enzyme from poppy seed was purified by ammonium sulphate precipitation and gel filtration chromatography. At the end of this study, lipase of poppy seed including 16,203 EU/mg protein, yield specific activity of 5,3 % and it is 22,29 times purified. For purified lipase from poppy seed expihibited the highest activity at optimum pH 13,2 and temperature 60 °C. The maximum activity stability is pH 7,2 and 4 °C. In order to determine the storage stability of lipase from poppy seed, the activity assays were performed for a period of two weeks. At the end of these two weeks it was observed that its activity of 61 % was retained at 4 °C. As the substrate of poppy seed lipase, triolein was used and Km and Vmax values were calculated. Consequenly Km 06,78 mM and Vmax 16,949 U/ dk.mg as enzyme were found. Key Words: Characterization, lipase, poppy seed, purification.