| Literature DB >> 25368146 |
Oscar Alvizo1, Luan J Nguyen2, Christopher K Savile3, Jamie A Bresson3, Satish L Lakhapatri4, Earl O P Solis2, Richard J Fox5, James M Broering6, Michael R Benoit3, Sabrina A Zimmerman7, Scott J Novick3, Jack Liang3, James J Lalonde3.
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 β-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.Entities:
Keywords: carbon capture; carbonic anhydrase; directed evolution
Year: 2014 PMID: 25368146 PMCID: PMC4246266 DOI: 10.1073/pnas.1411461111
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205