Immobilization to various carriers of purified lipase enzyme from chamomile (Matricaria chamomilla L.)

In this study, the immobilization of lipase enzyme, which has been purified for the first time, from chamomile (Matricaria chamomilla L.) grown in Giresun Province and its surroundings was investigated. Lipases (Triacylglycerol acyl hydrolase, E.C.3.1.1.3) are enzymes that catalyze the hydrolysis of triglycerides at the water-fat interface and have numerous applications in the industry. They have application areas in food, leather, detergent, paper, biomedical, biodiesel, biosensor, cosmetics and perfume industries. The use for various purposes in the chemical industry and in biotechnology of enzymes has necessitated making more economical and useful of these catalysts. In industrial processes, the immobilized lipase enzymes replaced of free lipase enzymes and increased its use. It was seen in literatüre studies that lipase enzyme has been purified from various plants but not purified from chamomile plants. Since it is thought to be an original work, it was aimed to purify from chamomile plant of lipase enzyme and increase its use by immobilizing to various carriers for the first time. In order to make enzymes more attractive in chemistry and biotechnology, studies on enzyme immobilization have intensified in the last 30 years. It is seen that the use of immobilized enzymes in industry in many fields has become widespread. The purified lipase was immobilized on the various carriers by adsorption, covalent and ionic bonding methods. Protein amount and lipase esterase activity were determined according to Lowry and Erlanson methods, respectively. Chamomile lipase was immobilized on various carriers (Kieselgel 60, sea sand, Amberlite IRA-900, alumina, glass beads) and it was investigated kinetic properties such as optimum pH, optimum temperature and optimum reaction time of immobilized lipases.