Kinetic Analysis of Immobilized Carbonic Anhydrase for Effective Environmental CO₂ Capture and Sequestration

Carbon capture and sequestration (CCS) is essential for mitigating climate change, with carbonic anhydrase (CA), a zinc metalloenzyme, emerging as a promising tool to enhance this process. CA facilitates the rapid conversion of CO<inf xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink">2</inf> to bicarbonate, a reaction crucial for both physiological functions and industrial applications. This study investigates the immobilization of bovine carbonic anhydrase on various materials, including polyurethane foam, calcium alginate beads, and chitosan beads, to improve its stability and effectiveness for CCS. The immobilized enzyme exhibited enhanced thermal and pH stability and improved kinetic performance compared to its free form. Key kinetic parameters, including the Michaelis-Menten constant (Km), maximum velocity (Vmax), turnover number (kcat), and specificity constant (kcat/Km), were evaluated to demonstrate these enhancements. The results underscore the potential of immobilized carbonic anhydrase in efficiently converting atmospheric CO<inf xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink">2</inf> into bicarbonate, presenting a viable approach for carbon sequestration and contributing to global greenhouse gas reduction efforts.