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


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.


Enzyme Spectroscopic Analysis Organic Chemistry Cysteine Penicillin 
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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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