Abstract
Lipases (triacylglycerol acylhydrolases, EC 3.1.1.3) catalyze the hydrolysis and the synthesis of esters formed from glycerol and long-chain fatty acids. Lipases occur widely in nature, but only microbial lipases are commercially significant. Many applications of lipases include specialty organic syntheses, hydrolysis of fats and oils, modification of fats, flavor enhancement in food processing, resolution of racemic mixtures, and chemical analyses. The aim of this study is to evaluate the biological importance of free and immobilized lipase enzyme. The support material used for lipase immobilization was sodium alginate with concentration 2%. Mostly, the immobilization of lipase in alginate gel exhibit more stability forheating than the free enzyme. The effect of metal ions Mg-2(+), Hg2+, Cu2+, Na+ andCa(2+)at a concentration 2 mol/ml used in the study showed inhibitory effect on free more than the immobilized lipase enzyme. These results highlighted the biochemical and technical advantage benefit of immobilized lipase over the free enzyme.