| 초록 |
In the biotechnology fields, carbonic anhydrase (CA) has been extensively investigated as a biocatalyst for CO2 sequestration—an advanced clean technology for the capture of excess CO2 from the atmosphere. CA (EC 4.2.1.1) is a zinc-containing metalloenzyme that catalyzes the reversible hydration of CO2 into bicarbonate and a proton, and can significantly enhance CO2 hydration. The presence of biocatalysts, CA can accelerate such CO2 mineralization that CA-mediated disposal of CO2 has been highlighted for economically-feasible and environmentally-benign system. However, for the practical use of CA for enzymatic CO2 sequestration system, high production and thrmostabilization of functional CAs should be achieved. Previously, we found that the N- and C-half CA domains of an internally duplicated, halo-tolerant α-type CA from Dunaliella sp (Dsp-CA) as distinct proteins. Although both proteins display structural similarity (51%) to the α–type CA (PDB ID: 1y7w), only the C-half CA domain (Dsp-CA-c) exhibited enzymatic activity. In the present study, chimeric proteins design strategy was employed for the increased soluble expression of Dsp-CA-c. |
