Enzymatic reaction kinetic: comparison in an organic solvent and in supercritical carbon dioxide.

Abstract:

:Myristic acid esterification has been performed by an immobilized lipase from Mucor Miehei both in n-hexane and in supercritical carbon dioxide (SCCO(2)). The enzyme is stable in SCCO(2) at 15 MPa and 323 K. The reaction rate is influenced by the concentration of water and by the reaction medium composition. A reaction mechanism is proposed, and kinetic parameters are determined at 12.5 MPa and 313 K. Maximum velocity appears 1.5-fold higher in SCCO(2) than in n-hexane; however, as solubility of myristic acid is greater in n-hexane, it is not yet definitively clear that the supercritical medium is more favorable than the classical organic solvent for this type of enzyme reaction.

journal_name

Biotechnol Bioeng

authors

Dumont T,Barth D,Corbier C,Branlant G,Perrut M

doi

10.1002/bit.260400218

subject

Has Abstract

pub_date

1992-06-20 00:00:00

pages

329-33

issue

2

eissn

0006-3592

issn

1097-0290

journal_volume

40

pub_type

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