Hydrolases in supercritical CO2 and their use in a high-pressure membrane reactor.

Abstract

The thermal stability and activity of enzymes in supercritical carbon dioxide (SC CO(2)) and near-critical propane were studied at a pressure of 300 bar in the temperature range 20-90 degrees C. Proteinase from Carica papaya was incubated in microaqueous SC CO(2) at atmospheric pressure in a nonaqueous system. Lipase stability in an aqueous medium at atmospheric pressure and in SC CO(2) as well as near-critical propane at 100 bar and 40 degrees C was studied. In order to investigate the impact of solvent on lipases, these were chosen from different sources: Pseudomonas fluorescences, Rhizpous javanicus, Rhizopus niveus and porcine pancreas. On the basis of our previous study on lipase activities in dense gases, a high-pressure continuous flat-shape membrane reactor was designed. The hydrolysis of sunflower oil in SC CO(2) was performed as a model reaction in this reactor. The reaction was catalyzed by the lipase preparation Lipolase 100T and was performed at 50 degrees C and 200 bar.