Abstract
The description of the kinetics of the enantiomeric resolution with lipases has been subject to study. The transesterification of (R,S)-1-phenyl ethanol using vinyl acetate in excess can be described as a pseudo-1-substrate reaction. The enantiomeric resolution with lipase from Penicillium cyclopium is based on a difference in conversion rate for the enantiomers. The binding rate on the enzymes is equal. Using lipase from Chromobacterium viscosum, kinetic resolution is obtained by a difference in binding rate, whilst the conversion rate for both enantiomers is equal. Uncompetitive inhibition is detected and validated in an enzymatic reaction model using reaction constants.
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References
Teeuwen, H. and Polastro E.T. (1990), Chiraliteit: Gouden berg of luchtkasteel voor de fijnchemische industrie, Chemisch Weekblad, 336–337 (In Dutch).
Zaks, A. and Klibanov, A.M. (1988), Enzyme catalysis in non aqueous solvents, J. Biol. Chem., 263. no 7, 3174–3201.
Adlercreuz, P. and Mattiasson, B. (1987), Aspects of biocatalyst stability in organic solvents, Biocatalysis, 1, 99–108.
Lattmann, R., Ghisalba, O., Gygax, D., Schar, H.P. and Schmidt, E. (1990), Screening and application of microbial esterases for the enantioselective synthesis of chiral glycerol derivatives, Biocatalysis, 3, 137–144.
Gais, H-J., Bulow, G., Zatorski, A., Jentsch, M., Maidonis, P. and Hemmerle H., (1989), Enzyme-catalyzed asymmetric synthesis. 8. Enantioselectivity of pig liver esterase catalyzed hydrolysis of 4-substituted meso cyclopentane 1,2-diesters, J. Org. Chem., 54, 5115–5122.
Ader, U., Breitgoff, D., Klein, P., Laumen, K.E. and Schneider, M.P. (1989), Enzymatic ester hydrolysis and synthesis — Two approaches to cycloalkane derivatives of high enantiomeric purity, Tetrahedon Letters, 30, no 14, 1793–1796.
Van Almsick, A., Buddris, J., Honicke-Schmidt, P. Laumen, K. and Schneider, M.P. (1989), Enzymatic preparation of optically active acetates, J. Chem. Soc. Commun., 1391.
Ahmar, M., Girard, C. and Bloch, R. (1989), Enzymatic resolution of methyl-2-alkyl-2-arylacetates, Tetrahedon Letters, 30, no 50, 7053–7056.
Kalaritus, P., Regenye, R.W., Partridge, J.J. and Coffen, D.L. (1990), Kinetic resolution of 2-substituted esters catalyzed by a lipase ex. Pseudomonas fluorescens, J. Org. Chem., 55, 812–815.
Tombo, G.M.R., Schär, H.-P. and Ghisalbo, O. (1987), Application of microbial esterases to the preparation of optically active N-acetylindoline-2-carboxylic acid, Agric. Biol. Chem., 51, no 7, 1833–1838.
Zaks, A. and Klibanov, A.M. (1984), Enzymatic catalysis in organic media at 100°C, Science, 224, 1249–1251.
Zaks, A., and Klibanov, A.M. (1985), Proc. Natl. Acad. Sci. USA, 82, 3192–3196.
Kirchner, G., Scollar, M.P. and Klibanov, M.A. (1985), Resolution of racemic mixtures via lipase catalysis in organic solvents, J. Am. Chem. Soc, 107, 7072,-7076.
Babiak, K.A., Ng, J.S., Dygos, J.H., Weyker, C.L., Wang, Y.F and Wong, C.-H. (1990), Lipasecatalyzed irreversible transesterification using enol esters: Resolution of prostaglandin synthons 4-hydroxy-2-alkyl-2-cyclopentenones and inversion of the 4S enantiomer to the 4R enantiomer, J. Org. Chem., 55, 3377–3381.
Van der Lugt, J.P. Elfrink, H., Evenaar, J. and Doddema, H.J. (1991), Enantiomeric separation with enzymes: Experimental research and simulation of enantioselective transesterification reactions in organic solvents, Proc. Second Int. Symp. on Chiral Discrimination, Roma, 109–110.
Deleuze, H., Langrand. G., Millet, H., Baratti, J., Buono, G., and Triantapylides, C. (1987), Lipase-catalyzed reactions in organic media: Competition and applications, Biochim. et Biophys. Acta, 811, 117–120.
Langrand, G., Baratti, J. and Triantapylides, C. (1988), Enzymatic separation and resolution of nucleophiles: A predictive kinetic model, Biocatalysis, 1, 231–248.
Chen, C.S., Fujimoto, Y., Girdaukas, G. and Sig, C.J. (1982), Quantitative analysis of biochemical kinetic resolution of enantiomers, J. Am. Chem. Soc., 104. 7294–7299.
Chen, C.-H., Wu, S.-H., Girdaukas, G. and Sih, C.J. (1987), Quantitative analysis of biochemical kinetic resolution of enantiomers. 2. Enzyme-catalyzed esterifications in water-organic solvent biphasic systems, J. Am. Chem. Soc., 109, 2812–2817.
Holmberg, E. and Hult, K. (1990), Transesterifications with Candida cylindracea lipase in a biphasic aqueous-organic system. Dependence of the enantiomeric ratio and the reaction rate in the proportion of water and cyclohexane, Biocatalysis, 3, 243–251.
Holmberg, E. and Hult, K. (1991), Temperature as an enantioselective parameter in enzymatic resolutions of racemic mixtures, Biotechnol. Letters, 13, no 5, 323–326.
Fitzpatrick, P.A. and Klibanov, M.A. (1991), How can the solvent affect enzyme enantioselectivity?, J. Am. Chem. Soc., 113, 3166–3171.
Tsai, S.-W. and Chiang, C.-L. (1991), Kinetics, mechanism, and time course analysis of lipase-catalyzed hydrolysis if high concentration olive oil in AOT-iso-octane reversed micelles, Biotechnol. Bioeng., 38, 206–211.
Bevinakatti, H.S., Banerji, A.A., Newadkar, R.V. and Mukesh, D. (1991), Mathematical modelling of lipase catalyzed resolution of O-acetyl and O-formyl derivatives of secondary alcohols, Biocatalysis, 5, 99–108.
Moressoli, C, Zaza, P., Flaschel, E. and Renken, A. (1992), Transesterification of phenylalanine by means of chymotrypsin in the presence of dimethyl sulfoxide, Biocatalysis, 5, 203–211.
Moressoli, C, Zaza, P., Flaschel, E. and Renken, A. (1992), The kinetics of transesterification by α-chymotrypsin of a racemic mixture of phenylalanine propyl ester with 1,4-butanediol, Biocatalysis, 5, 213–231.
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© 1992 Springer Science+Business Media Dordrecht
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van der Lugt, J.P., Elfrink, H., Evenaar, J., Doddema, H.J. (1992). Kinetics and Validation of Mathematical Models of Enantioselective Transesterification in Organic Solvents. In: Servi, S. (eds) Microbial Reagents in Organic Synthesis. NATO ASI Series, vol 381. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-2444-7_21
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DOI: https://doi.org/10.1007/978-94-011-2444-7_21
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