| dc.description.abstract | Carbon dioxide (CO2) has led to global warming and climate change, making sustainable development crucial in chemistry. Enzymes such as formate dehydrogenase (FDH) are essential for efficient CO2 fixation, converting it into organic biomaterials. indeed, enzyme instability and reusability limitations present challenges that impede practical applications. However, ongoing research seeks to surmount these obstacles and unleash the potential of enzymes for a more sustainable future. One effective approach to enhance enzyme stability is immobilizing enzymes on solid carriers. Metal-organic frameworks (MOFs), known for their emerging porous materials, create stable microenvironments that shield enzymes and prevent denaturation. Additionally, MOFs offer advantages such as high porosity, diverse synthesis conditions, and tunable structures, making them exceptionally promising carriers for enzyme immobilization.
In our laboratory, we have pioneered an innovative one-pot method to encapsulate catalase (CAT) enzyme within Zeolite Imidazolate Framework-90 (ZIF-90) in mild water conditions. This remarkable example of enzyme immobilization with MOFs has significantly improved enzyme stability and reusability. Moreover, MOFs, such as MOF-74, exhibit outstanding CO2 adsorption even in humid conditions, showing great potential for carbon capture and storage applications.
This research study utilized a rapid de novo synthesis method to encapsulate FDH within Zn-MOF-74 under mild aqueous conditions. Notably, this encapsulation process improves the enzyme′s acid-base tolerance, enabling it to remain active even at pH levels outside its non-active range, such as the pH = 6.1 of saturated carbon dioxide aqueous solution. The hexagonal channels and open metal sites of Zn-MOF-74 significantly enhance enzyme activity compared to the unencapsulated form, resulting in a remarkable three-fold increase in activity. | en_US |