Abstract
Different types of enzymes such as lipases, several phosphatases, dehydrogenases, oxidases, amylases and others are well suited for the reactions in SC-CO2. The stability and the activity of enzymes exposed to carbon dioxide under high pressure depend on enzyme species, water content in the solution and on the pressure and temperature of the reaction system. The three-dimensional structure of enzymes may be significantly altered under extreme conditions, causing their denaturation and consequent loss of activity. If the conditions are less adverse, the protein structure may be largely retained. Minor structural changes may induce an alternative active protein state with altered enzyme activity, specificity and stability.
Highlights
The finding that some enzymes, such as proteases, lipases, peroxidases, and esterases, are stable and active in organic solvents, has broadened immensely the scope of their applications as highly enantioselective catalysts in organic synthesis
These results suggest that this method enables the effective inactivation of enzymes, inactivation efficiency by this method was affected by initial pH and the buffer action of samples
(259 ± 9.0 kJ mol−1) of a heat treatment. These results indicated that a continuous treatment with micro-bubbles of SC-CO2 was more effective for enzyme inactivation
Summary
Institute of Experimental Botany AS CR, Isotope Laboratory, Vídeňská 1083, 142 20 Prague Institute of Organic Chemistry and Biochemistry AS CR, Flemingovo náměstí 2, 166 10 Prague Received: 23 November 2009; in revised form: 7 January 2010 / Accepted: 9 January 2010 /
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