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

► Carbonic anhydrase from bovine erythrocytes catalyzes the CO2 hydration efficiently. ► The enzyme was partially purified by extraction with solvents and by precipitation. ► Both techniques represent feasible alternatives for the industrial enzyme production. ► Purified enzyme showed the potential for use in carbon dioxide capturing processes. 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 2623UmL−1, recovery of 98% and purification factor of 104-fold. That precipitated by ammonium sulfate showed an activity of 2162UmL−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 CO2, but also promoted the formation of CaCO3.