Purification of lipase from Pistacia Terebinthus plant and studies of the kinetic properties

Lipase enzymes (triacyleglycerol acylhidrolase, EC.3.1.1.3), has wide aplication in industry because of their ability to catalyze hydrolysis, esterification, transesterification reactions. In recent years, lipase purification work has gained importance due to field and place of the use of lipase. In this study, purification and characterization of lipase enzyme from turpentine (Pistacia terebinthus) fruit has been intented. After deoiled of protein of turpentine furit, purification of the lipase was performed by gel filtration method. And the end of this study, lipase enzyme was purified 1.25 fold from turpentine fruit. Purified lipase enzyme shows maximum activity at pH 5,6 and 45 °C. Stable pH and stable temperature has been determined as 5.6 and 30 °C, respectively. The storage stability of turpentine furit lipase was determined for two weeks making activity measurements. At 4 °C and at the end of 16 days, enzyme activity has been observed that about 85% protection. It was calculated the KM and Vmax values of lipase from turpentine furit for triolein as substrate 0.2641mM and 9.107U/dk.mg enzyme, respectively. Key Words: Turpentine (Pistacia terebinthus) furit, lipase, purification, enzyme kinetics, characterization.