Purification and invesigation of kinetic properties of lipase enzyme from turpentine (Pistacia vera L.)

Enzymes with important metabolic functions for cellular structures have entered into everyday and economical life for various purposes. In recent years, the enzymatic modification of lipases and fats and oils has become increasingly important. Lipases used in almost every field of industry are usually obtained from microorganism and recently from oil seeds. Plant-derived lipases can be used in food, detergent and pharmaceutical industries, with advantages such as their easy availability, their high catalytic activity and their inability to form unwanted by-products. Due to the hydrolytic ability of oils, lipases are used as additives with the purpose of increasing cleaning effects in detergent products in households. . In this study, Antep peanut, which is an abundant fatty plant seed, was preferred and enzyme activities were determined as a result of the purification process. As a result of the degreasing process, the activity was measured as 5 ml NaOH. After the ammonium sulfate precipitation, the activity measurement was found to increase up to 8 ml NaOH. The stability and optimum temperature and pH values of Antep peanut plant seed lipase with determined kinetic properties were determined and compared with the kinetic properties of other lipase enzymes used in the detergent industry. The use of antep peanut lipase enzyme kinetics in the detergent industry has been found suitable. Key Words: Antep peanut (Pistacia vera), lipase enzyme, detergent industry, kinetic properties, characterization