Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/197236
Type: Artigo de periódico
Title: Kinetics Of Gas-phase Hydrolysis Of Ethyl Acetate Catalyzed By Immobilized Lipase.
Author: Perez, Victor H
Miranda, Everson A
Valença, Gustavo P
Abstract: 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.
Subject: Acetates
Enzyme Stability
Enzymes, Immobilized
Gases
Hydrolysis
Kinetics
Lipase
Partial Pressure
Reproducibility Of Results
Rights: fechado
Identifier DOI: 
Address: http://www.ncbi.nlm.nih.gov/pubmed/17416975
Date Issue: 2007
Appears in Collections:Artigos e Materiais de Revistas Científicas - Unicamp

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