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Title: Directed evolution of an ultrastable carbonic anhydrase for highly efficient carbon capture from flue gas

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. In conclusion, at pilot scale, the evolved catalyst enhanced the rate of CO2 absorption 25-fold compared with the noncatalyzed reaction.
Authors:
 [1] ;  [2] ;  [1] ;  [1] ;  [3] ;  [2] ;  [4] ;  [5] ;  [1] ;  [6] ;  [1] ;  [1] ;  [1]
  1. Codexis, Inc., Redwood City, CA (United States)
  2. Calysta Energy, Inc., Menlo Park, CA (United States)
  3. Siluria Technologies Inc., San Francisco, CA (United Sates)
  4. Pioneer Hi-Bred International, Inc., Johnston, IA (United States)
  5. Novosymes Inc, Franklinton, NC (United States)
  6. BP Biofuels, San Diego, CA (United States)
Publication Date:
Grant/Contract Number:
AR0000071
Type:
Accepted Manuscript
Journal Name:
Proceedings of the National Academy of Sciences of the United States of America
Additional Journal Information:
Journal Volume: 111; Journal Issue: 46; Journal ID: ISSN 0027-8424
Publisher:
National Academy of Sciences, Washington, DC (United States)
Research Org:
Codexis, Inc., Redwood City, CA (United States)
Sponsoring Org:
USDOE
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; carbon capture; directed evolution; carbonic anhydrase
OSTI Identifier:
1348349

Alvizo, Oscar, Nguyen, Luan J., Savile, Christopher K., Bresson, Jamie A., Lakhapatri, Satish L., Solis, Earl O. P., Fox, Richard J., Broering, James M., Benoit, Michael R., Zimmerman, Sabrina A., Novick, Scott J., Liang, Jack, and Lalonde, James J.. Directed evolution of an ultrastable carbonic anhydrase for highly efficient carbon capture from flue gas. United States: N. p., Web. doi:10.1073/pnas.1411461111.
Alvizo, Oscar, Nguyen, Luan J., Savile, Christopher K., Bresson, Jamie A., Lakhapatri, Satish L., Solis, Earl O. P., Fox, Richard J., Broering, James M., Benoit, Michael R., Zimmerman, Sabrina A., Novick, Scott J., Liang, Jack, & Lalonde, James J.. Directed evolution of an ultrastable carbonic anhydrase for highly efficient carbon capture from flue gas. United States. doi:10.1073/pnas.1411461111.
Alvizo, Oscar, Nguyen, Luan J., Savile, Christopher K., Bresson, Jamie A., Lakhapatri, Satish L., Solis, Earl O. P., Fox, Richard J., Broering, James M., Benoit, Michael R., Zimmerman, Sabrina A., Novick, Scott J., Liang, Jack, and Lalonde, James J.. 2014. "Directed evolution of an ultrastable carbonic anhydrase for highly efficient carbon capture from flue gas". United States. doi:10.1073/pnas.1411461111. https://www.osti.gov/servlets/purl/1348349.
@article{osti_1348349,
title = {Directed evolution of an ultrastable carbonic anhydrase for highly efficient carbon capture from flue gas},
author = {Alvizo, Oscar and Nguyen, Luan J. and Savile, Christopher K. and Bresson, Jamie A. and Lakhapatri, Satish L. and Solis, Earl O. P. and Fox, Richard J. and Broering, James M. and Benoit, Michael R. and Zimmerman, Sabrina A. and Novick, Scott J. and Liang, Jack and Lalonde, James J.},
abstractNote = {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. In conclusion, at pilot scale, the evolved catalyst enhanced the rate of CO2 absorption 25-fold compared with the noncatalyzed reaction.},
doi = {10.1073/pnas.1411461111},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
number = 46,
volume = 111,
place = {United States},
year = {2014},
month = {11}
}