Lipase Enzymes Purification from the Chamomile (Matricaria chamomilla L.) and Its Immobilization on Various Supports

In this study, lipase enzyme was firstly purified from chamomile (Matricaria chamomilla L.) which is abundant in Giresun (Turkey) and surroundings and the kinetic properties of the enzyme were investigated. 70 % of (NH4)2SO4 fraction of lipase esterase activity homogenate was obtained. After dialysis, this fraction was applied to DEAE-cellulose column, and lipase was purified 26 times. In the purification process, the protein amount was determined by using Lowry and E280/E260 Warburg methods while lipase esterase activtiy was assayed with Erlanson’s method. It was found that the purified enzyme, which obtained with SDS-PAGE electroforesis, had a molecular weight of 30 kDa. The optimum pH and temperature values were determined. It was found that the lipase purified from chamomile had an optimum pH value of 9 and an optimum temperature of 50 °C. When the affinity against different substrates of the enzyme was examined, the highest value was determined in p-nitrophenyl palmitate, with respectively Km and Vmax values being 0.2899 mM and 144.93 Units. Also, the lipase enzyme purified from chamomile was immobilized on various carriers by adsorption, covalent and ionic binding methods. The kinetic properties of the immobilized chamomile lipase such as optimum pH, optimum temperature were also studied