Enzyme denaturation in supercritical CO2: Stabilizing effect of S-S bonds during the depressurization step
- 122 Downloads
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.
KeywordsEnzyme Spectroscopic Analysis Organic Chemistry Cysteine Penicillin
Unable to display preview. Download preview PDF.
- van Eijs, A.M.M., and Oostrom, W.H.M., Abstracts IV the European Biotechnology Meeting June 1987 Amsterdam.Google Scholar
- Gabel, D., and Kasche, V. (1972).Acta Chem. Scand. 27, 1971–1981Google Scholar
- Hammond, D.A., Karel, M., Klibanov, A., and Krukonis, V. J., (1985).Appl. Biochem. Biotechnol. 11, 393–398Google Scholar
- Hoyer, G.G., (1985)Chemtec Juli 1985, 440–448Google Scholar
- Kasche, V., (1976)Arch. Biochem. Biophys.,173 269–272.Google Scholar
- Kasche, V., Haufler, U., Markowsky, D., Melnyk, S., Zeich, A., and Galunsky, B., (1987)Ann N.Y. Acad. Sci. 501, 97–102Google Scholar
- Kutzbach, C., and Rauenbusch, E., (1974)Hoppe Seyler's Z. Physiol. Chem. 354. 45–53Google Scholar
- Laemmli, U.K., (1970)Nature,227, 680–685Google Scholar
- Randolph, T.W., Blanch, H.W., Prausnitz, J.M., and Wilke, C.R., (1985)Biotechnol. Lett. 7, 325–329Google Scholar
- Randolph, T.W., Clark, D.S., Blanch, H.W. and Prausnitz, J.M., (1988)Science. 239, 387–390Google Scholar