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Enzymatic reaction kinetic: Comparison in an organic solvent and in supercritical carbon dioxide
Author(s) -
Dumont T.,
Barth D.,
Corbier C.,
Branlant G.,
Perrut M.
Publication year - 1992
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260400218
Subject(s) - supercritical carbon dioxide , carbon dioxide , supercritical fluid , chemistry , solvent , organic solvent , supercritical water oxidation , organic chemistry , kinetic energy , chemical engineering , physics , quantum mechanics , engineering
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. Maxium 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.

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