Immobilization of commercial lipase onto different supports: characterization and application in esterification reaction

Abstract— The current preference of costumers for natural and healthy products is increasing the employment of biotechnological processes that use enzymes, and the synthesis of esters is an example of this change. However, enzymes are high-cost product, which stimulates research in finding solutions that make them more economically attractive, like immobilization. This work aimed to use different protocols for immobilizing lipase and its application in ester synthesis. The results showed that Pseudomonas fluorences lipase (AKL) was the most efficient for immobilization among other studied lipases (Pseudomonas fluorences lipase (AKL), Pseudomonas cepacia lipase (PSL), Hog Pancreas lipase (PHL), Pancreas Porcinas lipase (PPL), and Mucor Javanicus lipase (MJL)), with hydrolytic activity of 3323.6 U/g. Both immobilization methods (physical adsorption and entrapment) showed promising results towards hydrolytic activity. The best immobilization by adsorption was obtained using AKL onto PHB (polyhydroxybutyrate), with 698.61 U/g of hydrolytic activity. For entrapment, AKL also presented the best result, with 247.30 U/g of hydrolytic activity. For the synthesis of ester, after a 60 h-reaction using the immobilized derivatives by physical adsorption, the esterification yield was 74.26 %. In terms of hydrolytic activity, the employed protocols were very promising and encourage the continuity of this study towards the optimization of processes using industrial lipases