Hostname: page-component-78c5997874-lj6df Total loading time: 0 Render date: 2024-11-15T22:32:11.711Z Has data issue: false hasContentIssue false
  • English
  • Français

Novel Polymer Synthesis using Enzymatic Catalysis in Nonaqueous Media

Published online by Cambridge University Press:  15 February 2011

Jonathan S. Dordick ,
Damodar. R. Patil ,
Keungarp Ryu  and
David G. Rethwisch
Jonathan S. Dordick
Affiliation:
Department of Chemical and Biochemical Engineering, University of Iowa, Iowa City, IA 52242.
Get access

Abstract

The use of enzymes in organic solvents has enabled two distinct polymer syntheses to be performed. The first is the enzyme-catalyzed polycondensation of sucrose with an adipic acid derivative in pyridine. Taking advantage of the extremely high regioselectivity of proleather, an alkaline protease, sucrose has been polymerized with 6 and 1' ester linkages. The result is a highly water-soluble product with sucrose an integral part of the polymer backbone. The polyester is degraded by the proleather in aqueous solution, thereby suggesting that the polymer is biodegradable. The second polymer synthesis is the free-radical polymerization of phenols using horseradish peroxidase in dioxane-water mixtures. Molecular weights in excess of 25,000 have been produced. The scope of polymerization can be predicted based on enzyme kinetics in organic media and using a Monte Carlo simulation. Astonishingly accurate simulations have been run that suggest that the high degree of control afforded by enzymatic catalysis over conventional chemical catalysts can be usedpredictively in polymer synthesis. This is of great importance in process control of polymer syntheses.

Type
Research Article
Information
MRS Online Proceedings Library (OPL) , Volume 218: Symposium V – Materials Synthesis Based on Biological Processes , 1990 , 17
Copyright
Copyright © Materials Research Society 1991

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

1. Notheisz, F. Bartok, M., and Remport, V.. Acta Phys. Chem. 18, 89–98 (1972).Google Scholar
2. Mosher, H.S. and Morrison, J.D.. Science, 221, 1013–1019 (1983).Google Scholar
3. Haines, A.H. Adv. Carbohydr. Chem. Biochem. 39, 13–70 (1981).Google Scholar
4. Desgupta, F., Hay, G.W., Szarek, W.A., and Schilling, W.L.. Carbohydr. Res. 114, 153–157 (1983).Google Scholar
5. Therisod, M. and Klibanov, A.M.. J. Am. Chem. Soc. 108, 5638–5640 (1986).CrossRefGoogle Scholar
6. Dordick, J.S., Hacking, A.J., and Khan, R.A.. U.S. Patent Pending.Google Scholar
7. Riva, S. and Klibanov, A.M.. J. Am. Chem. Soc. 110, 3291–3295 (1988).Google Scholar
8. Patil, D. R., Rethwisch, D. G., and Dordick, J. S.. Biotechnol. Bioeng. 37, 000-000 (in press).Google Scholar
9. Whitehouse, A.A.K., Pritchett, E.G.K., and Barnett, G.. Phenolic Resins. Chap. 2, Elsevier, New York (1968).Google Scholar
10. Marshall, E. Science, 237, 381 (1987).Google Scholar
11. Schwartz, R. D. and Hutchinson, D. B.. Enzyme Microb. Technol. 3, 361–363 (1981).Google Scholar
12. Dordick, J.S., Marietta, M.A., and Klibanov, A.M.. Biotechnol. Bioeng. 30, 31–36 (1987).Google Scholar
13. Pokora, A. R. and Cyrus, W. L.. U. S. Patent 4,647,952 (1987).Google Scholar
14. Ryu, K. and Dordick, J.S.. J. Am. Chem. Soc. 111, 8026–8027 (1989).Google Scholar