Enhancement of the catalytic activity of Carbonic Anhydrase by covalent immobilization on Magnetic Cellulose Crystals

In this study, Magnetic Cellulose Crystals (MCCs) are modified, characterized and used to immobilization of Bovine Carbonic Anhydrase (BCA). BCA enzyme was covalently attached via glutaraldehyde to two MCCs materials: a magnetic cellulose I polymorph (MCC-I) and a mixture of magnetic cellulose I and II polymorphs (MCC-I-II). The esterase activity of BCA immobilized into MCC-I (BCA-MCC-I) and MCC-I-II (BCA-MCC-I-II) was 228 and 318 % greater than the free enzyme, respectively. At 60 °C, BCA-MCC-I-II maintained up to 80 % of its initial activity, after 48 h. The activity of BCA-MCC-I was higher in comparison with the other derivatives at acid pH, conserved the 80 % of initial activity after 48 h. The high activity and stability of achieved biocatalysts are considering a great starting step to develop green strategies for CO2 mitigation, using eco-friendly materials, like cellulose. These findings are expected to impact enzyme-based CO2 transformation strategies and contribute to mitigate global warming. [Display omitted] •Bovine Carbonic Anhydrase (BCA) was immobilized on Magnetic Cellulose Crystal.•BCA biocatalysts changed its enzymatic performance due to the properties of carriers.•Higher activity was achieved when the BCA enzyme was immobilized on cellulose I.•The immobilized BCA on cellulose I-II exhibited the highest thermal stability at 60 °C.