Solvent induced change of enzyme enantioselectivity: Rule or exception?

Biocatalysis and Biotransformation

Volumn 15, Issue 3, 1997, Pages 175-184

  Wolff, A ^a   Straathof, A J J ^a   Jongejan, J A ^a   Heijnen, J J ^a  

^a DELFT UNIVERSITY OF TECHNOLOGY   (Netherlands)

Author keywords

Activity coefficient; Cosolvent; Enantioselectivity; Ethyl 3 phenyllactate; Kinetic resolution; Kinetics; UNIFAC; chymotrypsin

Indexed keywords

ACETIC ACID DERIVATIVE; CHYMOTRYPSIN; ETHYL 3 PHENYLACETATE; SOLVENT; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ENANTIOMER; ENZYME ACTIVITY; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HYDROLYSIS; MICHAELIS CONSTANT; THERMODYNAMICS;

EID: 0031433013     PISSN: 10242422     EISSN: None     Source Type: Journal    
DOI: 10.3109/10242429709103508     Document Type: Article

References (30)

1. Bell, R.P., Critchow, J.E. and Page, M.I. (1974) Ground state and transition state effects in the acylation of α - chymotrypsin in organic solvent water mixtures. J. Chem. Soc. Perkin Trans., 2, 66-70.
2. Carrea, G., Ottolina, G., Riva, S. and Secundo, F. (1992) Effect of reaction conditions on the activity and enantioselectivity of lipases in organic solvents. Prog. Biotechnol., 8, 339-346.
3. Carrea, G., Ottolina, G. and Riva, S. (1995) Role of solvents in the control of enzyme selectivity in organic media. Tibtech, 13, 63-70.
4. Chen, C.-S., Fujimoto, Y., Girdaukas, G. and Sih, C.J. (1982) Quantitative analyses of biochemical kinetic resolutions of enantiomers. J. Am. Chem. Soc., 104, 7294-7299.
5. Cohen, S.G. and Weinstein, S.Y. (1964) Hydrolysis of D-ethyl ß - phenyl - ß - hydroxypropionate and D-ethyl ß - phenyl - ß - acetamidopropionate by α - chymotrypsin. J. Am. Chem. Soc., 86, 725-728.
6. Dordick, J.S. (1992) Designing enzymes for use in organic solvents. Biotechnol. Prog., 8, 259-267.
7. Fredenslund, A., Gmehling, J. and Rasmussen, P. (1977) Vapor - Liquid Equilibria Using UNIFAC, Elsevier: New York.
8. Hailing, P.J. (1994) Thermodynamic predictions for biocatalysis in non-conventional media. Enzyme Microb. Technol., 16, 178-206.
9. Hansen, H.K.., Rasmussen, P., Schiller, M. and Gmehling, J. (1991) Vapor-liquid equilibria by UNIFAC group contribution: 5. revision and extension. Ind. Eng. Chem. Res., 30, 2352-2355.
10. Jones, J.B. and Mehes, M.M. (1979) Effects of organic cosolvents on enzyme stereospecificity. The enantiomeric specificity of α - chymotrypsin is reduced by high organic solvent concentrations. Can. J. Chem., 57, 2245-2248.
11. Jongejan, J.A., van Tol, J.B.A. and Duine, J.A. (1994) Enzymes in organic media: new solutions for industrial enzymatic catalysis. Chimicaoggi, 7, 15-24.
12. Ke, T., Wescott, C.R. and Klibanov, A.M. (1996) Prediction of the solvent dependence of enzymatic prochiral selectivity by means of structure-based thermodynamic calculations. J. Am. Chem. Soc, 118, 3366-3374.
13. Kezdy, F.J. and Kaiser, E.T. (1970) Principles of active site titration of proteolytic enzymes. Methods in Enzymology, 19, 3-20.
14. Khmelnitsky, Y.L., Mozhaev, V.V., Belova, A.B., Sergeeva, M.V. and Martinek, K. (1991) Denaturation capacity: a new quantitative criterion for selection of organic solvents as reaction media in biocatalysis. Eur. J. Biochem., 198, 31-41.
15. Maurel, P. (1978) Relevance of dielectric constant and solvent hydrophobicity to the organic solvent effect in enzymology. J. Biol. Chem., 253, 1677-1683.
16. Nakamura, K., Kinoshita, M. and Ohno, A. (1995) Structure of solvent affects enantioselectivity of lipase-catalyzed transesterification. Tetrahedron, 51, 8799-8808.
17. Parida, S. and Dordick, J.S. (1993) Tailoring lipase specificity by solvent and substrate chemistries. J. Org. Chem., 58, 3238-3244.
18. Rakels, J.L.L., Romein, B., Straathof, A.J.J. and Heijnen, J.J. (1994a) Kinetic analysis of enzymatic chiral resolution by progress curve evaluation. Biotechnol. Bioeng., 43, 411-422.
19. Rakels, J.L.L., Caillat, P., Straathof, A.J.J. and Heijnen. J.J. (1994b) Modification of the enzyme enantioselectivity by product inhibition. Biotechnol, Prog., 10, 403-409.
20. Sandler, S.I. (1989) Chemical and the Engineering Thermodynamics. Second edition, Wiley, New York
21. Sakurat, T., Margolin, A.L., Russell, A.L. and Klibanov, A.M. (1988) Control of enzyme enantioselectivity by the reaction medium. J. Am. Chem. Soc., 110, 7236-7237.
22. Schmitke, J.L., Wescott, C.R. and Klibanov, A.M. (1996) The mechanistic dissection of the plunge in enzymatic activity upon transition from water to anhydrous solvent. J. Am Chem. Soc., 118, 3360-3365.
23. Secundo, F., Riva, S. and Carrea, G (1992) Effects of medium and reaction conditions on the enantioselectivity of lipases in organic solvents and possible rationalities. Tetrahedron Asymmetry, 3, 267-280.
24. Smith, R.R. and Canady, W.J. (1992) Solvation effects upon the thermodynamic substrate activity; correlation with the kinetics of enzyme catalyzed reactions. I. Effects of added reagents such as methanol upon alpha-chymotrypsin. Biophysical Chemistry, 43, 173-187.
25. Straathof, A.J.J., Rakels, J.L.L. and Heijnen, J.J. (1992) Enzyme kinetics in monophasic and biphasic aqueous-organic systems. Prog. Biotechnol., 8, 137-144.
26. Tol, J.B.A., van, Odenthal, J.B., Jongejan, J.A. and Duine, J.A. (1992) Relation of enzymatic reaction rate and hydrophobicity of the solvent. Prog. Biotechnol., 8, 229-235.
27. Tomiuchi, Y., Kijima, T. and Kise, H. (1993) Fluorescence spectroscopic study of α - chymotrypsin as relevant to catalytic activity in aqueous-organic media. Bull. Chem. Soc. Jpn., 66, 1176-1181.
28. Wescott, C.R. and Klibanov, A.M. (1993) Solvent variation inverts substrate specificity of an enzyme. J. Am. Chem. Soc., 115, 1629-1631.
29. Wescott, C.R. and Klibanov, A.M. (1994) The solvent dependence of enzyme specificity Biochim. Biophys. Acta, 1206, 1-9.
30. Xu, Z.-F., Affleck, R., Wangikar, P., Suzawa, V., Dordick, J.S. and Clark, D.S. (1994) Transition state stabilization of subtilisins in organic media. Biotechnol. Bioeng., 43, 515-520.