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  • Purification of carbonic anhydrase from bovine erythrocytes and its application in the enzymic capture of carbon dioxide.

Purification of carbonic anhydrase from bovine erythrocytes and its application in the enzymic capture of carbon dioxide.

Chemosphere (2012-04-20)
Joana da Costa Ores, Luisa Sala, Guido Picaluga Cerveira, Susana Juliano Kalil
ZUSAMMENFASSUNG

This work presents a study of industrially applicable techniques to obtain a biologically supported carbon dioxide capture system, based on the extraction of carbonic anhydrase from bovine blood. Carbonic anhydrase is a metalloenzyme which catalyzes the reversible hydration of carbon dioxide. The objective of this study was to establish conditions to obtain carbonic anhydrase from bovine erythrocytes and apply it in the capture of carbon dioxide. To achieve this, two different purification techniques were evaluated: one by extraction with the organic solvents chloroform and ethanol, where different solvent proportions were studied; and the other by ammonium sulfate precipitation, testing percent saturations between 10% and 80%. Carbon dioxide was enzymatically captured by its precipitation as calcium carbonate with the enzyme obtained by both techniques. The enzyme extracted by ethanol and chloroform showed an activity of 2623 U mL(-1), recovery of 98% and purification factor of 104-fold. That precipitated by ammonium sulfate showed an activity of 2162 U mL(-1), recovery of 66% and purification factor of 1.4-fold using 60% ammonium sulfate saturation. The results obtained in the carbon dioxide capture experiments showed that the carbonic anhydrase extracted in this study not only enhanced the hydration of CO(2), but also promoted the formation of CaCO(3).

MATERIALIEN
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Produktbeschreibung

Sigma-Aldrich
Carboanhydrase aus Rindererythrocyten, ≥95% (SDS-PAGE), specific activity ≥3,500 W-A units/mg protein, lyophilized powder
Sigma-Aldrich
Carboanhydrase aus Rindererythrocyten, For use as a marker in SDS-PAGE
Sigma-Aldrich
Carbonic Anhydrase II bovine, ≥90% (SDS-PAGE), recombinant, expressed in E. coli, ≥5,000 units/mg protein, buffered aqueous solution