Kinetics of Gas-Phase Hydrolysis of Ethyl Acetate Catalyzed by Immobilized Lipase.

Victor H. Perez; Everson A. Miranda; Gustavo P. Valença

Reactions catalyzed by supported enzymes present important advantageswhen compared with those in aqueous media or organic solvents: separationof enzymes from substrate is easily accomplished, enzyme stability may beimproved, and control of the reaction products is more accurate. We presentthe experimental results of the kinetic study of ethyl acetate hydrolysis ingaseous phase catalyzed by a commercial immobilized lipase (Lipozyme IM;Novo Nordisk). The hydrolysis reaction was studied as a function of ethylester and water partial pressure at a constant temperature of 318 K. Theamount of biocatalyst used was varied between 100 and 300 mg, and thereaction was studied in a flow-through glass microreactor. Under the conditionsused, 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.

ENZYMES; PROTEINS; ETHYL acetoacetate; ORGANIC solvents

Applied Biochemistry & Biotechnology, 2007, Vol 136, Issue 1, p23

0273-2289

Academic Journal

10.1007/BF02685936