Carbonic anhydrase (CA) is an enzyme that rapidly catalyzes the reversible hydration of carbon dioxide (CO2). CA has been studied as a potential biocatalyst for CO2 capture and utilization. However, the application of CA to CO2 capture has been hampered by low thermostability and halotolerance of CA. Herein, a novel β-type CA from Thermovibiro ammonificans (β-TaCA) was studied as a promising enzyme for potential CO2 capture applications. The typical amino acid residues found in β-type CAs were conserved in β-TaCA. The solubility of β-TaCA was dependent on salt supplementation, requiring high salinities for conformational stability. The size exclusion chromatography revealed that the β-TaCA exists in a dimeric form. The zinc ion was detected at the active site as the catalytic metal ion. Interestingly, he two cysteine residues in the active site of β-TaCA was found to be in the oxidized state to form a disulfide bond in a significant fraction of enzyme molecules, thereby influencing the enzymatic activity of β-TaCA. The CO2 hydration activity of β-TaCA dramatically increased with increasing salt concentration. The enzyme showed an exceptional thermostability under high-salt conditions. In contrast to the other halophilic proteins with strongly negative surface charges, the β-TaCA showed a positive surface charges, which may be important for its halothermophilicity. In 20 wt% K2CO3, a widely used CO2 absorbent, the β-TaCA showed a superior kinetic stability to α-TaCA and DvCA10.0, the most thermostable CAs known to date, demonstrating the potential applicability of β-TaCA to CO2 capture. Collectively, these results demonstrate that the β-TaCA is an exceptionally thermostable and halophilic CA. Further efforts on engineering the enzyme stability will be required for the β-TaCA to be used as a practical biocatalyst for CO2 capture applications.