Unconventional Catalytic Properties of Conventional Enzymes: Applications in Organic Chemistry

  • Alexander M. Klibanov
Part of the Basic Life Sciences book series


The major objective of this paper is to stress that enzymes, in addition to their “normal” reactions (reflected in their names), often can catalyze other, sometimes quite different processes. The latter, although unimportant for the enzyme-producing organism, can be very valuable for biotechnological applications. The examples of “unnatural” catalytic activities of common enzymes that are considered, taken from the author’s recent studies, include: (i) reduction of aromatic compounds catalyzed by glucose oxidase; (ii) prochiral and enantiomeric stereospecificity of galactose oxidase in the oxidation of non-sugar, three-carbon alcohols; (iii) selective hydroxylation of aromatic compounds catalyzed by peroxidase; (iv) geometrically and positionally specific oxidation of aromatic aldehydes catalyzed by xanthine oxidase.

It is pointed out that along with conventional bacterial screening, a “chemical screening”, i.e., the search for new, unconventional catalytic activities for known enzymes, can be beneficial.


Xanthine Oxidase Glucose Oxidase Trans Isomer Aromatic Aldehyde Ascorbate Oxidase 
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.


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  1. 1.
    Enzyme Nomenclature. 1979. Academic Press, New York.Google Scholar
  2. 2.
    Schmid, R. D. 1979. Oxidoreductases present and potential applications in technology. Process Biochem. 14 (6): 27.Google Scholar
  3. 3.
    Dawson, C. R., 1966. Ascorbate oxidase: a review. In Peisach, P. Aisen, and W.E. Blumberg (eds.), The Biochemistry of Copper, pp 305–337. Academic Press, New York.Google Scholar
  4. 4.
    Bright, H. J., D. J. T. Porter. 1975. Flavoprotein oxidases, chapter 7. In P.D. Boyer (ed.), The Enzymes, 3rd ed., vol. 12. Academic Press, New York.Google Scholar
  5. 5.
    Whitaker, J. R. 1972. Principles of enzymology for the food sciences, chapter 21. M. Dekker, New York.Google Scholar
  6. 6.
    Scott, D., 1975. Applications of glucose oxidase, chapter 19. In G. Reed (ed.), Enzymes in Food Processing, 2nd ed. Academic Press, New York.Google Scholar
  7. 7.
    Dixon, M., E. C. Webb. 1979. Enzymes, 3rd ed., pp. 243–244. Academic Press, New York.Google Scholar
  8. 8.
    Carr, P. W. L. D. Bowers, 1980. Immobilized enzymes in analytical and clinical chemistry, chapter 5. Wiley, New York.Google Scholar
  9. 9.
    Guilbault, G. G. 1980. Immobilized enzymes as analytical rea gents. Appl. Biochem. Biotechnol. 7: 85–98.CrossRefGoogle Scholar
  10. 10.
    Keilin, D., E. F., Hartree. 1948. Properties of glucose oxidase. Biochem. J. 42: 221–229.Google Scholar
  11. 11.
    Alberti, B. N., A. M. Klibanov, 1982. Preparative production of hydroquinone from benzoquinone catalyzed by immobilized glucose oxidase. Enzyme Microb. Technol. 4: 47–49.Google Scholar
  12. 12.
    Hamilton, G. A., J. DeJersey, P. K. Adolf, 1973. Galactose oxidase: the complexities of a simple enzyme, pp. 103124. In T.E. King, H.S. Mason, and M. Morrison (ed.), Oxidases and related redox systems, vol. 1. University Park Press, Baltimore.Google Scholar
  13. 13.
    Klibanov, A. M., B. N. Alberti, M. A. Marietta, 1982. Stereo-specific oxidation of aliphatic alcohols catalyzed by galactose oxidase. Biochim. Biophys. Acta, submitted for publication.Google Scholar
  14. 14.
    Saunders, B. C., A. G. HolmesSiedle, B. P. Stark, 1964. Peroxidase. Butterworth, London.Google Scholar
  15. 15.
    Klibanov, A. M., B. N. Alberti, E. D. Morris, L. M. Felshin, 1980. Enzymatic removal of toxic phenols and anilines from waste waters. J. Appl. Biochem. 2: 414–421.Google Scholar
  16. 16.
    Alberti, B. N., A. M. Klibanov, 1981. Enzymatic removal of dissolved aromatics from industrial aqueous effluents. Biotechnol. Bioeng. Symp. 11: 373–379.Google Scholar
  17. 17.
    Mason, H. S., I. Onopryenko, and Buhler, D. 1957. Hydroxylation: the activation of oxygen by peroxidase. Biochim. Biophys. Acta 24: 225–226.CrossRefGoogle Scholar
  18. 18.
    Buhler, D., H. S. Mason, 1961. Hydroxylation catalyzed by peroxidase. Arch. Biochem. Biophys. 92: 424–437.CrossRefGoogle Scholar
  19. 19.
    Daly, J.W., D. M. Jerina, 1970. Aerobic aromatic hydroxylation catalyzed by horseradish peroxidase: absence of NIH shift. Biochim. Biophys. Acta 208: 340–342.CrossRefGoogle Scholar
  20. 20.
    Klibanov, A. M., Z. Berman, B. N. Alberti,, 1981. Preparative hydroxylation of aromatic compounds catalyzed by peroxidase. J. Amer. Chem. Soc. 103: 6263–6264.CrossRefGoogle Scholar
  21. 21.
    Massey, V., 1973. Ironsulfur flavoprotein hydroxylases, pp. 301–360. In W. Lovenberg (ed.), Ironsulfur proteins, vol. 1. Academic Press, New York, New York.Google Scholar
  22. 22.
    Booth, V. H., 1938. The specificity of xanthine oxidase. Biochem. J. 32: 494–502.Google Scholar
  23. 23.
    Klibanov, A. M., P. P. Giannousis, 1982. Geometrically specific oxidation of β-arylacroleins catalyzed by xanthine oxidase: the preparative potential. Biotechnol. Lett, hi 57–60.Google Scholar
  24. 24.
    Klibanov, A. M., E. H. Siegel, 1982. Geometric specificity of porcine liver carboxyl esterase and its application for the production of cis-arylacrylic esters. Enzyme Microb. Technol. 4: 172–174.Google Scholar
  25. 25.
    Klibanov, A. M., P. P. Giannousis, 1982. Geometric specificity of alcohol dehydrogenases and its potential for separation of trans and cis isomers of unsaturated aldehydes. Proc. Natl. Acad. Sci. USA 79: 3462–3465.CrossRefGoogle Scholar
  26. 26.
    Pelsy, G., A. M. Klibanov, 1982. Remarkable positional (regio) specificity of xanthine oxidase and some dehydrogenases in the reactions with substituted benzaldehydes. Biochemistry 21:submitted for publication.Google Scholar

Copyright information

© Plenum Press, New York 1983

Authors and Affiliations

  • Alexander M. Klibanov
    • 1
  1. 1.Laboratory of Applied Biochemistry Department of Nutrition and Food ScienceMassachusetts Institute of TechnologyCambridgeUSA

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