Kinetics of gas-phase hydrolysis of ethyl acetate catalyzed by immobilized lipase.
Reactions catalyzed by supported enzymes present important advantages when compared with those in aqueous media or organic solvents: separation of enzymes from substrate is easily accomplished, enzyme stability may be improved, and control of the reaction products is more accurate. We present the experimental results of the kinetic study of ethyl acetate hydrolysis in gaseous phase catalyzed by a commercial immobilized lipase (Lipozyme IM; Novo Nordisk). The hydrolysis reaction was studied as a function of ethyl ester and water partial pressure at a constant temperature of 318 K. The amount of biocatalyst used was varied between 100 and 300 mg, and the reaction was studied in a flow-through glass microreactor. Under the conditions used, water was an important parameter in the gas-phase reaction. Activation energy was 24.8 kJ/mol and the overall order of reaction was one. Finally, a Bi-Bi reaction mechanism is proposed.
Perez
Victor H
VH
Department of Biotechnological Processes, School of Chemical Engineering, State University of Campinas, PO Box 6066, 13083-970, Campinas-SP, Brazil. victorh@fea.unicamp.br
Miranda
Everson A
EA
Valença
Gustavo P
GP
D000085:Acetates / Q000378:metabolism*; D004795:Enzyme Stability; D004800:Enzymes, Immobilized / Q000378:metabolism*; D005740:Gases; D006868:Hydrolysis; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D010313:Partial Pressure; D015203:Reproducibility of Results
D000085:Acetates; D004800:Enzymes, Immobilized; D005740:Gases; C007650:ethyl acetate; C093666:Lipozyme; D008049:Lipase