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Biotechnology Letters

, Volume 10, Issue 8, pp 569–574 | Cite as

Enzyme denaturation in supercritical CO2: Stabilizing effect of S-S bonds during the depressurization step

  • Volker Kasche
  • Ralf Schlothauer
  • Gerd Brunner
Article

Summary

The stability of the monomeric enzymes α-chymotrypsin and trypsin, and the oligomeric enzyme penicillin amidase in supercritical CO2 has been studied. They were found to be partly denatured during the depressurization step. The degree of denaturation was larger in humid CO2 than in dry CO2. Enzymes with S-S bridges (α-chymotrypsin; trypsin) were denatured to a lesser degree than the enzyme without cysteine (penicillin amidase). These results and electrophoretic and spectroscopic analysis indicated that the denaturation was caused by partial unfolding during the depressurization step.

Keywords

Enzyme Spectroscopic Analysis Organic Chemistry Cysteine Penicillin 
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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References

  1. van Eijs, A.M.M., and Oostrom, W.H.M., Abstracts IV the European Biotechnology Meeting June 1987 Amsterdam.Google Scholar
  2. Gabel, D., and Kasche, V. (1972).Acta Chem. Scand. 27, 1971–1981Google Scholar
  3. Hammond, D.A., Karel, M., Klibanov, A., and Krukonis, V. J., (1985).Appl. Biochem. Biotechnol. 11, 393–398Google Scholar
  4. Hoyer, G.G., (1985)Chemtec Juli 1985, 440–448Google Scholar
  5. Kasche, V., (1976)Arch. Biochem. Biophys.,173 269–272.Google Scholar
  6. Kasche, V., Haufler, U., Markowsky, D., Melnyk, S., Zeich, A., and Galunsky, B., (1987)Ann N.Y. Acad. Sci. 501, 97–102Google Scholar
  7. Kutzbach, C., and Rauenbusch, E., (1974)Hoppe Seyler's Z. Physiol. Chem. 354. 45–53Google Scholar
  8. Laemmli, U.K., (1970)Nature,227, 680–685Google Scholar
  9. Randolph, T.W., Blanch, H.W., Prausnitz, J.M., and Wilke, C.R., (1985)Biotechnol. Lett. 7, 325–329Google Scholar
  10. Randolph, T.W., Clark, D.S., Blanch, H.W. and Prausnitz, J.M., (1988)Science. 239, 387–390Google Scholar

Copyright information

© Kluwer Academic Publishers 1988

Authors and Affiliations

  • Volker Kasche
    • 1
  • Ralf Schlothauer
    • 1
  • Gerd Brunner
    • 2
  1. 1.AB Biotechnologie IITechnische Universität Hamburg-HarburgHamburg 90FRG
  2. 2.AB Verfahrenstechnik IITechnische Universität Hamburg-HarburgHamburg 90FRG

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