http://www.cnr.it/ontology/cnr/individuo/prodotto/ID238395

Performance of a Biphasic Organic/Aqueous Hollow Fiber Reactor Using Immobilized Lipase (Articolo in rivista)

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Performance of a Biphasic Organic/Aqueous Hollow Fiber Reactor Using Immobilized Lipase (Articolo in rivista) (literal)

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Alternative label

L. Giorno, R. Molinari, E. Drioli, D. Bianchi, P. Cesti (1995)
Performance of a Biphasic Organic/Aqueous Hollow Fiber Reactor Using Immobilized Lipase
in Journal of chemical technology and biotechnology (1979); John Wiley & Sons Ltd., Chichester (Regno Unito)
(literal)

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Titolo

Performance of a Biphasic Organic/Aqueous Hollow Fiber Reactor Using Immobilized Lipase (literal)

Abstract

A biphasic organic/aqueous membrane bioreactor, which combined chemical reaction with continuous extraction of production in the aqueous phase, was investigated. Lipase from Candida Cylindracea was used as catalyst with the hydrolysis of triglycerides, to fatty acids and glycerol, as a model-system for studying the optimal operating conditions. Asymmetric capillary membranes, made of polyamide, were used as support for the enzyme, which was immobilized into the sponge layer of the membrane by cross-flow filtration. The catalytic behavior of lipase, both immobilized in a hydrophilic membrane and free in solution, was compared. The effect of pH, temperature and substrate concentration on reactor performance were studied. The catalytic stability of the immobilized enzyme was improved compared with the enzyme in solution. The immobilized lapse showed no deactivating in an operating period of 16 days whereas lipase in solution gave an 80% decrease in specific activity after 2 days of continuous operation. The specific activity of immobilized lipase was significantly influenced by the amount of enzyme loaded into the membranes. The optimal range of immobilized protein was between 2 and 12 mg cm-3. The positive results obtained with the model-system were also confirmed using the biphasic organic/aqueous membrane bioreactor in a potential practical application, namely the conversion and separation of one enantiomer from an organic racemic mixture of an ester. (literal)

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