碳酸酐酶和甲酸脱氢酶的稳定性研究进展

The massive combustion of fossil fuels increases the emission of the greenhouse gas CO₂, which has a bad impact on the environment. The capture and conversion of CO₂ into high value-added chemicals is a win-win strategy to achieve energy conservation and emission reduction and turn waste into treasure. Enzyme-catalyzed CO₂ capture and conversion has such advantages as high efficiency, high selectivity, mild reaction conditions, and environmental friendliness. Carbonic anhydrase (CA) can greatly accelerate CO₂ hydration reaction, while formate dehydrogenase (FDH) can catalyze the reduction of CO₂ to formate, and the synergy of CA and FDH can enhance CO₂ reduction kinetics. However, in the industrial application of enzymatic reactions, factors such as temperature, pH, and the type and concentration of other ions may lead to the inactivation of the enzyme. Therefore, the study on the enzyme stability is vital. In this review, the research progress of the stability of CA and FDH and the effect of immobilization on the stability of enzymes are reviewed from the perspectives of thermal stability, acid-base stability and ionic stability. Strategies for improving the enzyme stability include the use of extremophiles, the rational design and modification of enzyme molecules, in which the effect of the immobilization method on the stability of enzyme is elaborated, providing reference for future industrial applications.