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

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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.

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Authors and Affiliations

  1. AB Biotechnologie II, Technische Universität Hamburg-Harburg, Postfach 90 14 03, D-2100, Hamburg 90, FRG

    Volker Kasche & Ralf Schlothauer

  2. AB Verfahrenstechnik II, Technische Universität Hamburg-Harburg, Postfach 90 14 03, D-2100, Hamburg 90, FRG

    Gerd Brunner

Authors
  1. Volker Kasche
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  2. Ralf Schlothauer
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  3. Gerd Brunner
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Kasche, V., Schlothauer, R. & Brunner, G. Enzyme denaturation in supercritical CO2: Stabilizing effect of S-S bonds during the depressurization step. Biotechnol Lett 10, 569–574 (1988). https://doi.org/10.1007/BF01027131

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  • DOI: https://doi.org/10.1007/BF01027131

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