(323e) Metal Organic Frameworks Promise High Activity and Stability of Carbonic Anhydrase in Synthetic Environment
Carbonic anhydrase (CA) has shown great potential for carbon dioxide (CO2) sequestration and transformation due to its ultrahigh turnover. However, the fragile nature of the free enzyme significantly limits its application in industry. Herein we propose to develop robust CA-based biocatalyst for CO2 sequestration and transformation based on metal organic frameworks (MOFs). For this, we employed a hydrophilic and a hydrophobic MOF support for CA immobilization and evaluated the support characteristics that will ensure maximum functionality and stability of the enzyme. MOFs' morphology, crystallinity and particle size were evaluated by scanning electron microscopy (SEM), dynamic light scattering (DLS) and X-Ray diffraction (XRD) respectively and compared with the characteristics of the conjugates. Analysis showed that the supports influenced both the enzyme loading and activity, as well as determined enzyme kinetics and stability at interfaces. Further, results showed that controlling the hydrophilicity of the support could lead to not only increased enzyme functionality but further, increased stability relative to that of free enzyme. These results point to MOFs having a high potential to fill in the gap for developing sensitive supports with tunable hydration conditions that allow for high enzyme activity and stability retention and hint at extended implementation capability when CO2 storage and transformation based on enzyme-imposed green technologies is considered.