ABSTRACT
Carbonic anhydrase (CA) is one of nature's fastest enzymes and can dramatically improve the economics of carbon capture under demanding environments such as coal-fired power plants. The use of CA to accelerate carbon capture is limited by the enzyme's sensitivity to the harsh process conditions. Using directed evolution, the properties of a ß-class CA from Desulfovibrio vulgaris were dramatically enhanced. Iterative rounds of library design, library generation, and high-throughput screening identified highly stable CA variants that tolerate temperatures of up to 107 °C in the presence of 4.2 M alkaline amine solvent at pH >10.0. This increase in thermostability and alkali tolerance translates to a 4,000,000-fold improvement over the natural enzyme. At pilot scale, the evolved catalyst enhanced the rate of CO2 absorption 25-fold compared with the noncatalyzed reaction.
ABSTRACT
The potential for enzymatic acceleration of carbon dioxide capture from combustion products of fossil fuels has been demonstrated. Carbonic anhydrase (CA) accelerates post combustion CO(2) capture, but available CAs are woefully inadequate for the harsh conditions employed in most of these processes. In this review, we summarize recent approaches to improve CA, and processes employing this enzyme, to maximize the benefit from this extremely fast biocatalyst. Approaches to overcoming limitations include sourcing CAs from thermophilic organisms, using protein engineering to evolve thermo-tolerant enzymes, immobilizing the enzyme for stabilization and confinement to cooler regions and process modifications that minimize the (thermo-, solvent) stress on the enzyme.
