Biocatalytic CO(2) Absorption and Structural Studies of Carbonic Anhydrase under Industrially-Relevant Conditions

The unprecedently high CO(2) levels in the atmosphere evoke the urgent need for development of technologies for mitigation of its emissions. Among the alternatives, the biocatalytic route has been claimed as one of the most promising. In the present work, the carbonic anhydrase from bovine erythrocytes (BCA) was employed as a model enzyme for structural studies in an aqueous phase at alkaline pH, which is typical of large-scale absorption processes under operation. Circular dichroism (CD) analysis revealed a high enzymatic stability at pH 10 with a prominent decrease of the melting temperature above this value. The CO(2) absorption capacity of the aqueous solutions were assessed by online monitoring of pressure decay in a stainless-steel cell, which indicated a better performance at pH 10 with a kinetic rate increase of up to 43%, as compared to non-biocatalytic conditions. Even low enzyme concentrations (0.2 mg g(−1)) proved to be sufficient to improve the overall CO(2) capture process performance. The enzyme-enhanced approach of CO(2) capture presents a high potential and should be further studied.