Membrane reactor with immobilized Candida antarctica lipase B for ester synthesis in supercritical carbon dioxide

Immobilized Candida antarctica lipase B (CALB) was successfully used as catalyst to synthesize butyl butyrate from butyl vinyl ester and 1-butanol in supercritical carbon dioxide (scCO 2) with excellent results. The catalytic behaviour of the enzyme immobilized on an acrylic support has been studied...

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Bibliographic Details
Published in:	The Journal of supercritical fluids Vol. 29; no. 1; pp. 121 - 128
Main Authors:	Lozano, P, Vı́llora, G, Gómez, D, Gayo, A.B, Sánchez-Conesa, J.A, Rubio, M, Iborra, J.L
Format:	Journal Article
Language:	English
Published:	Elsevier B.V 01-04-2004
Subjects:	Candida antarctica lipase B Ester synthesis Lipase Membrane reactor Supercritical fluids Candida antarctica lipase B Membrane reactor Supercritical fluids Ester synthesis Lipase
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Summary:	Immobilized Candida antarctica lipase B (CALB) was successfully used as catalyst to synthesize butyl butyrate from butyl vinyl ester and 1-butanol in supercritical carbon dioxide (scCO 2) with excellent results. The catalytic behaviour of the enzyme immobilized on an acrylic support has been studied in a stirred tank reactor, showing that a decrease in both the water content and the scCO 2 density enhanced the synthetic activity and selectivity (>99.0%). Then, ceramic membranes were coated with hydrophilic polymers, and then used to covalently attach CALB. These active membranes were applied for continuous butyl butyrate synthesis in a cross-flow reactor with different organic solvents and supercritical conditions, as reaction media. A clear enhancement in the synthetic activity and selectivity was observed with the decrease in fluid density for both liquids and scCO 2 media. However, all supercritical conditions assayed enhanced up 84-folds respect to the organic solvents the synthetic activity of the lipase-membrane derivative. For the best supercritical conditions (60 °C, 8 MPa), the enzymatic membrane was assayed by repetitive operational cycles of 6 h/day, showing a 360 cycles half-life time in their synthetic activity.
ISSN:	0896-8446 1872-8162
DOI:	10.1016/S0896-8446(03)00050-0