N. Saini, S. Kalyaanamoorthy
University of Waterloo,
Canada
Keywords: Enzyme, CO2 capture, Biocatalyst
Summary:
The escalating emission of CO2 due to fossil fuel consumption and its consequential impact on climate change underscore the urgent necessity for efficient CO2 capture methods. Carbonic anhydrases, a group of ancient and fastest known enzymes, catalyzing the reversible hydration of CO2 to bicarbonate, have emerged as pivotal biocatalysts for CO2 capture. However, the utilization of CAs in enhancing the carbon capture process is hampered by the natural enzymes’ susceptibility to harsh conditions prevalent in industrial settings. Hence, there is an imperative need to engineer these enzymes with high stability and catalytic performance. Various approaches have been previously employed to engineer CAs, aiming to enhance their thermal stability and activity. In this study, we have engineered a novel CA endowed with extraordinary thermostability and enhanced activity through computational design. The designed CA exhibits substantial augmented activity, characterized by a kcat of 4.3 X 10^7 sec-1, along with exceptional thermostability exceeding 100°C. Furthermore, the reconstructed enzyme displayed reversible thermal renaturation, with retained catalytic functionality. Temperature-dependent activity revealed that the designed CA maintains remarkable enzymatic activity at 100°C, surpassing the performance of most natural CAs documented in the literature. Collectively, our study presents a novel biocatalyst with promising prospects for the development of enzyme-based CO2 capture strategies.