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Enzymic catalysis in supercritical carbon dioxide

Marie Zarevúcka 1Roumiana P. Stateva 2

1. Czech Academy of Sciences, Institute of Organic Chemistry and Biochemistry, Flemingovo n. 2, Prague 16610, Czech Republic
2. Institute of Chemical Engineering, Bulgarian Academy of Sciences, Academic Georgi Bontchev str., bl. 103, Sofia 1113, Bulgaria

Abstract

We outlined three main tasks: each one of them included one or more subprojects and was aligned with one of the participating research groups, a condition which proved to be critical for the achievement of the goals envisaged.

(i) Testing the enzyme activity and stability in supercritical carbon dioxide.

Two types of enzymes (lipase and glucose 2-oxidase from Coriolus versicolor) were tested under SC-CO2 from the point of view of enzyme stability and enzyme specificity.

(ii) Investigating the enzyme reaction in continuous-flow reactor, conversion of the reactions and specificity of enzymes

Two model reactions were tested: 1) hydrolysis of blackcurrant oil by lipase from Mucor miehei immobilized on macroporous anionic resin (Lipozyme®) and lipase from Geotrichum candidum, 2) the oxidation of D-.glucose at carbon 2 in the presence of molecular oxygen producing D-glucosone (2-keto-glucose and D-arabino-2-hexosulose) and hydrogen peroxide catalysed by glucose 2-oxidase. The processes in respect of the products of the reaction were optimised.

(iii) Understanding the kinetic, thermodynamic, and transport phenomena which influence the enzyme-catalyzed reactions

Particular attention was given to studying and modeling the kinetics of the enzyme-catalysed reactions, and to modeling the simultaneous phase and chemical equilibrium.

Acknowledgement: The authors appreciate financial support from the Ministry of Education of the CR through the COST project D30/0008/06 (COST D30.001).

 

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Related papers

Presentation: Invited at COST D30 Final Evaluation Meeting, by Marie Zarevúcka
See On-line Journal of COST D30 Final Evaluation Meeting

Submitted: 2007-10-05 15:20
Revised:   2014-10-06 14:03