Advertisement

Enzymes at Oil-Water Interfaces and in Organic Solvents

  • Daniel A. Abramowicz
  • Charles R. Keese

Summary

Enzymes act as remarkably efficient catalysts in biological systems. Some characteristics of enzymes such as their chiral specificity for some substrates make them attractive catalysts for chemical synthesis. Many desirable substrates, however, have poor solubility in the aqueous systems normally employed with most enzymatic reactions. The use of isolated enzymes in organic solvent systems can overcome this problem and offer new possibilities for enzyme use in chemical synthesis. In addition to making substrates with low aqueous solubility available to the enzyme, organic systems can enable enzymatic catalysis at low water concentrations (<0.05%) where new reactions are possible.

We have used a lipase from Candida cyclindracea and other esterases to hydrolyze a novel water-insoluble substrate (diphenyl carbonate, DPC) in miscible organic solutions and at oil-water interfaces. We have achieved turnovers of >2000/enzyme/min in these systems with a crude enzyme preparation. We have also observed transesterification of diphenyl carbonate (DPC) with a wide variety of alcohol (ROH) and phenol (ArOH) species.

Keywords

Transesterification Reaction Crude Enzyme Preparation Organic Solvent System Transesterification Activity Diphenyl Carbonate 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Whitesides, G.M. and Wong, C.H.(1983) Aldrichimica Acta, 16, 27–34Google Scholar
  2. 2.
    Jones, J.B. (1985) in: Enzymes in Organic Synthesis”, Pitman Press, Bath, Great Britain, pp. 3–14Google Scholar
  3. 3.
    Fuganti, C. and Grasselli, P. (1985) in:Enzymes in Organic Synthesis, Pitman Press, Bath, Great Britain, pp. 112–125Google Scholar
  4. 4.
    Cambou, B. and Klibanov, A.M. (1984) J. Am. Chem. Soc., 106, 2687–2692CrossRefGoogle Scholar
  5. 5.
    Butler, L.G. (1979) Enzyme Microb. Technol. 1, 253–259CrossRefGoogle Scholar
  6. Gatfield, I.L. (1984) Ann. N.Y. Acad. Sci., 434, 569–572CrossRefGoogle Scholar
  7. 7.
    Fruton, J.S. (1982) in:Adv. Enzymology, A. Meister (ed.) John Wiley and Sons, New York, vol. 53, pp. 239–306Google Scholar
  8. 8.
    Zaks, A. and Klibanov, A.M. (1984) Science, 224, 1249–1251CrossRefGoogle Scholar
  9. 9.
    Laemmli, U.K. (1970) Nature, 227, 680–685CrossRefGoogle Scholar
  10. 10.
    Fefer, J. and Giaver, I. (1980) J. Coll. Interf. Sci., 79, 144–154Google Scholar
  11. 11.
    Ouellette, R.P. and Cheremisinoff, P.N. (1985) “ Essentials of Biotechnology”, Technimic Publishing Co., Lancaster, PA, USA, pp. 69–71Google Scholar

Copyright information

© Plenum Press, New York 1987

Authors and Affiliations

  • Daniel A. Abramowicz
    • 1
  • Charles R. Keese
    • 1
  1. 1.General Electric Research and Development CenterSchenectadyNew YorkUSA

Personalised recommendations