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

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America
 [1];  [2];  [3];  [3];  [4];  [2];  [5];  [6];  [3];  [7];  [3];  [3];  [3]
  1. Codexis, Inc., Redwood City, CA (United States); DOE Office of Scientific and Technical Information (OSTI)
  2. Calysta Energy, Inc., Menlo Park, CA (United States)
  3. Codexis, Inc., Redwood City, CA (United States)
  4. Siluria Technologies Inc., San Francisco, CA (United Sates)
  5. Pioneer Hi-Bred International, Inc., Johnston, IA (United States)
  6. Novosymes Inc, Franklinton, NC (United States)
  7. BP Biofuels, San Diego, CA (United States)
+ Show Author Affiliations

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.

Research Organization:
Codexis, Inc., Redwood City, CA (United States)
Sponsoring Organization:
USDOE
Grant/Contract Number:
AR0000071
OSTI ID:
1348349
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America, Journal Name: Proceedings of the National Academy of Sciences of the United States of America Journal Issue: 46 Vol. 111; ISSN 0027-8424
Publisher:
National Academy of Sciences, Washington, DC (United States)Copyright Statement
Country of Publication:
United States
Language:
English

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Cited By (22)

The carbonic anhydrase of Clostridium autoethanogenum represents a new subclass of β-carbonic anhydrases journal July 2019
Engineering de novo disulfide bond in bacterial α-type carbonic anhydrase for thermostable carbon sequestration journal July 2016
The Hitchhiker's guide to biocatalysis: recent advances in the use of enzymes in organic synthesis journal January 2020
Production and covalent immobilisation of the recombinant bacterial carbonic anhydrase (SspCA) onto magnetic nanoparticles journal January 2017
Cloning, Over-Expression, and Purification of β–Carbonic Anhydrase from an Extremophilic Bacterium: Deinococcus radiodurans journal May 2021
Microbial Carbonic Anhydrases in Biomimetic Carbon Sequestration for Mitigating Global Warming: Prospects and Perspectives journal August 2017
Thermostable Carbonic Anhydrases in Biotechnological Applications journal July 2015
Characterization and High-Level Periplasmic Expression of Thermostable α-Carbonic Anhydrase from Thermosulfurimonas Dismutans in Escherichia Coli for CO2 Capture and Utilization journal December 2019
Immobilization of Carbonic Anhydrase in Glass Micropipettes and Glass Fiber Filters for Flow-Through Reactor Applications text January 2018
ARduino‐pH Tracker and screening platform for characterization of recombinant carbonic anhydrase in Escherichia coli journal May 2019
The carbonic anhydrase of Clostridium autoethanogenum represents a new subclass of β-carbonic anhydrases journal July 2019
Expression of an Environmentally Friendly Enzyme, Engineered Carbonic Anhydrase, in Escherichia coli journal March 2019
The limits to biocatalysis: pushing the envelope journal January 2018
A call to (green) arms: a rallying cry for green chemistry and engineering for CO 2 capture, utilisation and storage journal January 2018
Structural and biophysical characterization of the α-carbonic anhydrase from the gammaproteobacterium Thiomicrospira crunogena XCL-2: insights into engineering thermostable enzymes for CO 2 sequestration journal July 2015
Identification of a new thermostable and alkali-tolerant α-carbonic anhydrase from Lactobacillus delbrueckii as a biocatalyst for CO2 biomineralization journal November 2015
Characterization of a hyperthermophilic phosphatase from Archaeoglobus fulgidus and its application in in vitro synthetic enzymatic biosystem journal June 2019
Kinetic Study of CO2 Hydration by Small-Molecule Catalysts with A Second Coordination Sphere that Mimic the Effect of the Thr-199 Residue of Carbonic Anhydrase journal October 2019
Sustainable Recycling of Formic Acid by Bio-Catalytic CO2 Capture and Re-Hydrogenation journal May 2019
Recent Progress and Novel Applications in Enzymatic Conversion of Carbon Dioxide journal April 2017
Thermostable Carbonic Anhydrases in Biotechnological Applications journal July 2015
Characterization and High-Level Periplasmic Expression of Thermostable α-Carbonic Anhydrase from Thermosulfurimonas Dismutans in Escherichia Coli for CO2 Capture and Utilization journal December 2019

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60 APPLIED LIFE SCIENCES
carbon capture
carbonic anhydrase
directed evolution