Skip to main content

Thank you for visiting You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • Research Article
  • Published:

Biocatalytic plastics as active and stable materials for biotransformations


Enzyme-containing polymeric materials have been developed that have high activity and stability in both aqueous and organic media. These biocatalytic plastics, containing α-chymotrypsin and subtilisin Carlsberg, can contain up to 50% (w/w) total protein in plastic materials such as poly(methyl methacrylate, styrane, vinyl acetate, and ethyl vinyl ether). The activation achieved in organic solvents by incorporating proteases in plastic matrices allows for the efficient synthesis of peptides, and sugar and nucleoside esters. The marriage of enzyme technology with polymer chemistry opens up an array of unique applications for plastic enzymes, including active and stable biocatalysts in paints, coatings, resins, foams, and beads, as well as membranes, fibers, and tubings.

This is a preview of subscription content, access via your institution

Access options

Buy this article

Prices may be subject to local taxes which are calculated during checkout

Similar content being viewed by others


  1. Blanch, H.W. and Clark, D.S. 1995. Biochemical Engineering. Marcel Dekker, New York, NY.

    Google Scholar 

  2. Wiseman, A. 1985. Handbook of Enzyme Biotechnology, 2nd ed., Ellis Harwood, Ltd., New York, NY.

    Google Scholar 

  3. Clark, D.S. 1994. Prospects for exploiting immobilization to modify enzyme activity. Trends. Biotechnol. 12: 439.

    Article  CAS  Google Scholar 

  4. Martinek, K., Klibanov, A.M., Goldmacher, V.S. and Berezin, I.V. 1977. The principles of enzyme stabilization I. Increase in thermostability of enzymes covalently bound to a complementary surface of a polymer support in a multipoint fashion. Biochim. Biophys. Acta 485: 1–12.

    Article  CAS  Google Scholar 

  5. Dordick, J.S. 1989. Enzymatic catalysis in monophasic organic solvents. Enzyme Microb. Technol. 11: 194–211.

    Article  CAS  Google Scholar 

  6. Takahashi, K., Ajima, A., Yoshimoto, T., Okada, M., Matsushima, A., Tamaura, Y. and Inada, Y. 1985. Chemical reactions by polyethylene glycol modified enzymes in chlorinated hydrocarbons. J. Org. Chem. 50: 3414–3415.

    Article  CAS  Google Scholar 

  7. Pina, C., Clark, D.S. and Blanch, H.W. 1989. The activity of PEG-modified chymotrypsin in aqueous and organic media. Biotechnol. Blotechniq. 3: 333–338.

    Article  CAS  Google Scholar 

  8. Yang, Z., Mesiano, A.J., Venkatasubramanian, S., Gross, S.H., Harris, J.M. and Russell, A.J. 1995. Activity and stability of enzymes incorporated into acrylic polymers. J. Am. Chem. Soc. 117: 4843–4850.

    Article  CAS  Google Scholar 

  9. Ito, Y., Fujii, H. and Imanishi, Y. 1993. Catalytic peptide synthesis by trypsin modified with polystyrene in chloroform. Biotechnol. Prog. 9: 128–130.

    Article  CAS  Google Scholar 

  10. Ito, Y., Fujii, H. and Imanishi, Y. 1992. Enzyme hybridization with synthetic polymers for use in organic media. Makromol. Chem. Rapid Commun. 13: 315–319.

    Article  CAS  Google Scholar 

  11. Paradkar, V.M. and Dordick, J.S. 1994. Aqueous-like activity of α-chymotrypsin dissolved in nearly anhydrous organic solvents. J. Am. Chem. Soc. 116: 5009–5010.

    Article  CAS  Google Scholar 

  12. Paradkar, V.M. and Dordick, J.S. 1994. Extraction and solubilization of chymotrypsin into isooctane in the presence of low concentrations of aerosol OT in the absence of reversed micelles. Biotechnol. Bioeng. 43: 529–540.

    Article  CAS  Google Scholar 

  13. Matsuura, J., Powers, M.E., Manning, M.C. and Shefter, E. 1993. Structure and stability of insulin dissolved in 1-octanol. J. Am. Chem. Soc. 115: 1261–1264.

    Article  CAS  Google Scholar 

  14. Meyer, J.D., Matsuura, J.E., Kendrick, B.S., Evans, E.S., Evans, G.J. and Manning, M.C. 1995. Solution behavior of α-chymotrypsin dissolved in nonpolar organic solvents via hydrophobic ion-pairing. Biopolymers 35: 451–456.

    Article  CAS  Google Scholar 

  15. Klibanov, A.M. 1990. Asymmetric transformations catalyzed by enzymes in organic solvent. Ace. Chem. Res. 23: 114–120.

    Article  CAS  Google Scholar 

  16. Tramper, J., VermŸe, M.H., Beeftink, H.H. and von Stockar, U. (eds.). 1992. Biocatalysis in Non-cotiventional Media. Elsevier, Amsterdam, The Netherlands.

    Google Scholar 

  17. Odian, G. 1991. Principles of Polymerization. John Wiley & Sons, Inc. New York.

    Google Scholar 

  18. Gabel, D. 1974. Active site titration of immobilized chymotrypsin with a fluorogenic reagent. FEBS Letters 49: 280–281.

    Article  CAS  Google Scholar 

  19. Allcock, H.R. and Lampe, F.W. 1990. Contemporary Polymer Chemistry. PrenticeHall, Inc., Englewood Cliffs, NJ.

    Google Scholar 

  20. Wangikar, P.P., Michels, P.C., Clark, D.S. and Dordick, J.S. 1997. Structure and function of subtilisin BPŃ solubilized in organic solvents. J. Am. Chem. Soc. 119: 70–76.

    Article  CAS  Google Scholar 

  21. Stepanov, V.M. 1996. Proteinases as catalysts in peptide synthesis. Pure and Applied Chemistry 68: 1335–1339.

    Article  CAS  Google Scholar 

  22. Rich, J.O., Bedell, B.A. and Dordick, J.S. 1995. Controlling enzyme-catalyzed regioselectivity in sugar ester synthesis. Biotechnol. Bioeng. 45: 426–434.

    Article  CAS  Google Scholar 

  23. Moris, F. and Gotor, V. 1993. A useful and versatile procedure for the acylation of nucleosides through an enzymatic reaction. J. Org. Chem. 58: 653–660.

    Article  CAS  Google Scholar 

  24. Rich, J.O. and Dordiok, J.S. 1996. Controlling regioselectivity in enzyme-catalyzed acylation of polyhydroxyl compounds. Ann. N.Y. Acad. Sci. 799: 226–230.

    Article  CAS  Google Scholar 

  25. Fields, R. 1971. The measurement of amino groups in proteins and peptides. Biochem. J. 124: 581–590.

    Article  CAS  Google Scholar 

  26. Orthgeiss, E. and Dobias, B. 1990. Colorimetric determination of anionic surfactants. Biotechnol. Bioeng. 40: 91–102.

    Google Scholar 

  27. Wangikar, P.P., Carmichael, D., Clark, D.S. and Dordick, J.S. 1995. Active site titration of serine protaases in organic solvents. Biotechnol. Bioeng. 50: 329–335.

    Article  Google Scholar 

Download references

Author information

Authors and Affiliations


Corresponding author

Correspondence to Jonathan S. Dordick.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Wang, P., Sergeeva, M., Lim, L. et al. Biocatalytic plastics as active and stable materials for biotransformations. Nat Biotechnol 15, 789–793 (1997).

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI:

This article is cited by


Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing