Biotechnology Letters

, Volume 24, Issue 11, pp 857–860 | Cite as

A caveat for the use of log P values for the assessment of the biocompatibility of organic solvents

  • Mateja Pogorevc
  • Hartmut Stecher
  • Kurt Faber


The degree of enzyme deactivation for lipases from Candida rugosa and Pseudomonas sp., hydroxynitrile lyase and mandelate racemase upon exposure to organic solvents can be correlated to their respective partition coefficients (log P values). However, three unexpected results were obtained: (1) the deactivation exerted by protic solvents, e.g., methanol, is severely underestimated; (2) little deactivation by an organic solvent cannot neccessarily be correlated to catalytic activity in this medium, and (3) in contrast to other enzymes, hydroxynitrile lyase is exceptionally stable towards deactivation by DMF.

enzyme deactivation hydroxynitrile lyase lipase log P mandelate racemase 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. Adlercreutz P, Mattiasson B (1987) Aspects of biocatalyst stability in organic solvents. Biocatalysis 1: 99-108.Google Scholar
  2. Andersson M, Holmberg H, Adlercreutz P (1998) Prediction of the remaining activity of horse liver alcohol dehydrogenase after exposure to various organic solvents. Biocatal. Biotransfor. 16: 259-273.Google Scholar
  3. Bauer C, Boy M, Faber K, Felfer U, Voss H (2001) Activation of mandelate racemase via immobilisation in lyotropic liquid crystals for biocatalysis in organic solvents: application and modelling. J. Mol. Catal. B 16: 91-100.Google Scholar
  4. Carrea G, Riva S (2000) Properties and synthetic applications of enzymes in organic solvents. Angew. Chem., Intern. Ed. 39: 2226-2254.Google Scholar
  5. Colton IJ, Ahmed SN, Kazlauskas RJ (1995) A 2-propanol treatment increases the enantioselectivity of Candida rugosa lipase towards esters of chiral carboxylic acids. J. Org. Chem. 60: 212-217.Google Scholar
  6. Faber K, Ottolina G, Riva S (1993) Selectivity enhancement of hydrolase reactions. Biocatalysis 8: 91-132.Google Scholar
  7. Fitzpatrick PA, Klibanov AM (1991) How can the solvent affect enzyme enantioselectivity? J. Am. Chem. Soc. 113: 3166-3171.Google Scholar
  8. Gruber K, Gugganig M, Wagner UG, Kratky C (1999) Atomic resolution crystal structure of hydroxynitrile lyase from Hevea brasiliensis. Biol. Chem. 380: 993-1000.Google Scholar
  9. Halling PJ (1994) Thermodynamic predictions for biocatalysis in nonconventional media: theory, tests, and recommendations for experimental design and analysis. Enzyme Microb. Technol. 16: 178-206.Google Scholar
  10. Hasslacher M, Schall M, Hayn M, Griengl H, Kohlwein SD, Schwab H (1996) Molecular cloning of the full-length cDNA of (S)-hydroxynitrile lyase from Hevea brasiliensis. J. Biol. Chem. 271: 5884-5891.Google Scholar
  11. Laane C, Boeren S, Vos K, Veeger C (1987) Rules for optimization of biocatalysts in organic solvents. Biotechnol. Bioeng. 30: 81-87.Google Scholar
  12. Stecher H, Felfer U, Faber K (1997) Large-scale production of mandelate racemase by Pseudomonas putida ATCC 12633: optimization of enzyme induction and development of a stable crude enzyme preparation. J. Biotechnol. 56: 33-40.Google Scholar
  13. Stecher H, Hermetter A, Faber K (1998) Mandelate racemase assayed by polarimetry. Biotechnol. Tech. 12: 257-261.Google Scholar
  14. Weber HK, Stecher H, Faber K (1999) Some properties of commercially available crude lipase preparations. In: Roberts SM, ed. Biocatalysts for Fine Chemicals Synthesis. Chichester: Wiley, module 5:2.1.Google Scholar

Copyright information

© Kluwer Academic Publishers 2002

Authors and Affiliations

  • Mateja Pogorevc
    • 1
  • Hartmut Stecher
    • 1
  • Kurt Faber
    • 1
  1. 1.Department of Chemistry, Organic & Bioorganic ChemistryUniversity of GrazGrazAustria

Personalised recommendations