Techno-Economic Analysis of Biocatalytic Processes for Production of Alkene Epoxides

Chapter
Part of the ABAB Symposium book series (ABAB)

Abstract

A techno-economic analysis of two different bioprocesses was conducted, one for the conversion of propylene to propylene oxide (PO) and other for conversion of styrene to styrene epoxide (SO). The first process was a lipasemediated chemo-enzymatic reaction, whereas the second one was a one-step enzymatic process using chloroperoxidase. The PO produced through the chemo-enzymatic process is a racemic product, whereas the latter process (based on chloroperoxidase) produces an enantio-pure product. The former process thus falls under the category of high-volume commodity chemical (PO); whereas the latter is a low-volume, high-value product (SO).

A simulation of the process was conducted using the bioprocess engineering software SuperPro Designer v6.0 (Intelligen, Inc., Scotch Plains, NJ) to determine the economic feasibility of the process. The purpose of the exercise was to compare biocatalytic processes with existing chemical processes for production of alkene expoxides. The results show that further improvements are needed in improving biocatalyst stability to make these bioprocesses competitive with chemical processes.

Index Entries

Bioprocess chloroperoxidase economics enzymatic epoxides lipase 
This is a preview of subscription content, log in to check access.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. 1.
    Adamczak, M. and Krishna, S. H. (2004), Food Technol. Biotechnol. 42, 251–264.Google Scholar
  2. 2.
    Gupta, M. N. and Roy, I. (2004), Eur. J. Biochem. 271, 2575–2583.CrossRefGoogle Scholar
  3. 3.
    D’Souza, S. F. (1999), Curr. Sci. 77, 69–79.Google Scholar
  4. 4.
    Dai, L. Z. and Klibanov, A. M. (1999), Proc. Natl. Acad. Sci. USA 96, 9475–9478.CrossRefGoogle Scholar
  5. 5.
    Morgan, J. A. and Clark, D. S. (2004), Biotechnol. Bioeng. 85, 456–459.CrossRefGoogle Scholar
  6. 6.
    Sawae, H., Sakoguchi, A., Nakashio, F., and Goto, M. (2002), J. Chem. Eng. Japan 35, 677–680.CrossRefGoogle Scholar
  7. 7.
    Song, B. D., Ding, H., Wu, J. C., Hayashi, Y., Talukder, M., and Wang, S. C. (2003), Chin. J. Chem. Eng. 11, 601–603.Google Scholar
  8. 8.
    Mine, Y., Fukunaga, K., Yoshimoto, M., Nakao, K., and Sugimura, Y. (2001), J. Biosci. Bioeng. 92, 539–543.CrossRefGoogle Scholar
  9. 9.
    Wang, L. F., Zhu, G. Y., Wang, P., and Newby, B. M. Z. (2005), Biotechnol. Prog. 21, 1321–1328.CrossRefGoogle Scholar
  10. 10.
    Panke, S., Wubbolts, M. G., Schmid, A., and Witholt, B. (2000), Biotechnol. Bioeng. 69, 91–100.CrossRefGoogle Scholar
  11. 11.
    Bjorkling, F., Frykman, H., Godtfredsen, S. E., and Kirk, O. (1992), Tetrahedron 48, 4587–4592.CrossRefGoogle Scholar
  12. 12.
    Bjorkling, F., Godtfredsen, S. E., and Kirk, O. (1990), J. Chem. Soc. Chem. Commun. 19, 1301–1303.CrossRefGoogle Scholar
  13. 13.
    Klaas, M. R. G. and Warwel, S. (1997), J. Mol. Catalysis a-Chem. 117, 311–319.CrossRefGoogle Scholar
  14. 14.
    Archelas, A. and Furstoss, R. (1997), Ann. Rev. Microbiol. 51, 491–525.CrossRefGoogle Scholar
  15. 15.
    Chem Systems, Inc. Report, Assessment of the likely role of biotechnology in commodity chemical production (1988), 20–97, Tarrytown, NY.Google Scholar
  16. 16.
    Soni, B. K., Kelley, R. L., and Srivastava, V. J. (1998), Appl. Biochem. Biotechnol. 74, 115–123.CrossRefGoogle Scholar
  17. 17.
    Hilker, I., Bothe, D., Pruss, J., and Warnecke, H. J. (2001), Chem. Eng. Sci. 56, 427–432.CrossRefGoogle Scholar
  18. 18.
    Klaas, M. R. and Warwel, S. (1999), Ind. Crops Prod. 9, 125–132.CrossRefGoogle Scholar
  19. 19.
    Sober, H. A. and Harte, R. A. (eds.) (1970), Handbook of Biochemistry, 2nd ed. The Chemical Rubber Co., Cleveland, OH: pp. E10–E21.Google Scholar
  20. 20.
    Park, J. B. and Clark, D. S. (2006), Biotechnol. Bioeng. 93, 1190–1195.CrossRefGoogle Scholar
  21. 21.
    Park, J. B. and Clark, D. S. (2006), Biotechnol. Bioeng. 94, 189–192.CrossRefGoogle Scholar
  22. 22.
    Panke, S., Held, M., Wubbolts, M. G., Witholt, B., and Schmid, A. (2002), Biotechnol. Bioeng. 80, 33–41.CrossRefGoogle Scholar
  23. 23.
    van de Velde, F., Bakker, M., van Rantwijk, F., Rai, G. P., Hager, L. P., and Sheldon, R. A. (2001), J. Mol. Catalysis B-Enzymatic 11, 765–769.CrossRefGoogle Scholar
  24. 24.
    Andersson, M., Andersson, M. M., and Adlercreutz, P. (2000), Biocatalysis Biotransform. 18, 457–469.CrossRefGoogle Scholar
  25. 25.
    Conesa, A., van de Velde, F., van Rantwijk, F., Sheldon, R. A., van den Hondel, C., and Punt, P. J. (2001), J. Biol. Chem. 276, 17,635–17,640.CrossRefGoogle Scholar
  26. 26.
    Rai, G. P., Zong, Q., and Hager, L. P. (2000), Isr. J. Chem. 40, 63–70.CrossRefGoogle Scholar
  27. 27.
    Ayala, M., Horjales, E., Pickard, M. A., and Vazquez-Duhalt, R. (2002), Biochem. Biophys. Res. Commun. 295, 828–831.CrossRefGoogle Scholar
  28. 28.
    Borole, A., Dai, S., Cheng, C. L., Rodriguez, M., and Davison, B. H. (2004), Appl. Biochem. Biotechnol. 113–116, 273–285.CrossRefGoogle Scholar
  29. 29.
    van Rantwijk, F. and Sheldon, R. A. (2000), Curr. Opin. Biotechnol. 11, 554–564.CrossRefGoogle Scholar

Copyright information

© Humana Press Inc. 2007

Authors and Affiliations

  1. 1.Life Biosciences DivisionOak Ridge National LaboratoryOak Ridge

Personalised recommendations