Enzymatic Activity of Immobilized Carbonic Anhydrase onto Amberlite XAD7

Carbon capture by using carbonic anhydrase (CA) enzyme has become an alternative and environmental friendly approach in carbon sequestration technology. Among various form of CA, immobilized CA onto the support materials offer better behaviour of enzyme including enhance enzyme stability, increase biocatalytic activity and improved enzyme reusability. These factors are important in carbon sequestration in order to reduce the operation cost and achieve optimum CO2 utilization. Thus, behaviour of the CA immobilized onto the solid support is important in order to determine its activity towards CO2 capture. In this study, different initial concentration of CA immobilized onto amberlite XAD7 was investigated for the optimum CO2 sequestration through protein analysis and enzyme activity towards p-NPA substrate. The CA initial concentration was varied from 0.32 to 1.87 mg/ml while other parameters were kept constant where temperature at 25°C, speed shaking at 100 rpm, pH at 8.0 and support dosage at 0.5g. The CA initial concentration at 0.32 mg/ml gave the highest percentage of immobilized enzyme (99%). While, the highest enzyme activity towards its substrate obtained was 1.58mmol/min using 99% CA attached to amberlite XAD7.