Lipase purification from the seeds of chestnut (Castanea sativa) and its immobization on various supports

Lipases are enzymes whose systematic name is triacylglycerol acylhydrolase which is able to catalyze the hydrolysis of triacylglycerols in aqueous medium to convert di and monoacylglycerols and glycerol to ester bonds in anhydrous medium In order to make the enzymes more attractive in the field of chemistry and biotechnology, the focus has been on enzyme immobilization in the last 30 years. The use of immobilized enzymes seems to be widespread across the industry. In this study, it is aimed to investigate the immobilization and kinetics of lipase enzyme purified from chestnut (Castanea sativa) seeds by adsorption, covalent and ionic binding methods to various carriers. The kinetic properties of the immobilized lipase enzyme were examined and compared with the free lipase enzyme. Purified lipase was immobilized on various supports by adsorption, covalent and ionic attachment methods. In the purification process, the protein content was determined by using Lowry method, and lipase esterase activtiy was assayed with Erlanson's method. Immobilization of the lipase purified from chestnut seeds on several supports (Silikagel, seasand, Amberlite IRA-900, alumina, glass beads), kinetic properties such as optimum pH and temperature, optimum reaction time were also examined.