The use of carbonic anhydrase to accelerate carbon dioxide capture processes

2014 ◽  
Vol 90 (1) ◽  
pp. 3-10 ◽  
Author(s):  
Joel K. J. Yong ◽  
Geoff W. Stevens ◽  
Frank Caruso ◽  
Sandra E. Kentish
Keyword(s):  
Carbon Dioxide ◽  
Carbonic Anhydrase ◽  
Carbon Dioxide Capture

Carbon dioxide capture usingEscherichia coliexpressing carbonic anhydrase in a foam bioreactor

2016 ◽  
Vol 37 (24) ◽  
pp. 3186-3192 ◽  
Author(s):  
Stuart K. Watson ◽  
Zhenlin Han ◽  
Wei Wen Su ◽  
Marc A. Deshusses ◽  
Eunsung Kan
Keyword(s):  
Carbon Dioxide ◽  
Carbonic Anhydrase ◽  
Carbon Dioxide Capture

scholarly journals The structure of a tetrameric α-carbonic anhydrase fromThermovibrio ammonificansreveals a core formed around intermolecular disulfides that contribute to its thermostability

2014 ◽  
Vol 70 (10) ◽  
pp. 2607-2618 ◽  
Author(s):  
Paul James ◽  
Michail N. Isupov ◽  
Christopher Sayer ◽  
Vahid Saneei ◽  
Svein Berg ◽  
...  
Keyword(s):  
Carbon Dioxide ◽  
Carbonic Anhydrase ◽  
Carbon Dioxide Capture ◽  
Carbonic Anhydrases ◽  
Native Form ◽  
Industrial Carbon ◽  
E Coli ◽  
Reducing Environment ◽  
Reversible Hydration ◽  
Unique Core

Carbonic anhydrase enzymes catalyse the reversible hydration of carbon dioxide to bicarbonate. A thermophilicThermovibrio ammonificansα-carbonic anhydrase (TaCA) has been expressed inEscherichia coliand structurally and biochemically characterized. The crystal structure of TaCA has been determined in its native form and in two complexes with bound inhibitors. The tetrameric enzyme is stabilized by a unique core in the centre of the molecule formed by two intersubunit disulfides and a single lysine residue from each monomer that is involved in intersubunit ionic interactions. The structure of this core protects the intersubunit disulfides from reduction, whereas the conserved intrasubunit disulfides are not formed in the reducing environment of theE. colihost cytosol. When oxidized to mimic the environment of the periplasmic space, TaCA has increased thermostability, retaining 90% activity after incubation at 70°C for 1 h, making it a good candidate for industrial carbon-dioxide capture. The reduction of all TaCA cysteines resulted in dissociation of the tetrameric molecule into monomers with lower activity and reduced thermostability. Unlike other characterized α-carbonic anhydrases, TaCA does not display esterase activity towardsp-nitrophenyl acetate, which appears to result from the increased rigidity of its protein scaffold.

Enzymatic carbon dioxide capture using a thermally stable carbonic anhydrase as a promoter in potassium carbonate solvents

2017 ◽  
Vol 307 ◽  
pp. 49-55 ◽  
Author(s):  
Guoping Hu ◽  
Kathryn H. Smith ◽  
Nathan J. Nicholas ◽  
Joel Yong ◽  
Sandra E. Kentish ◽  
...  
Keyword(s):  
Carbon Dioxide ◽  
Carbonic Anhydrase ◽  
Potassium Carbonate ◽  
Carbon Dioxide Capture ◽  
Thermally Stable

scholarly journals Enzymatic Carbon Dioxide Capture

2012 ◽  
Vol 2012 ◽  
pp. 1-22 ◽  
Author(s):  
Alain C. Pierre
Keyword(s):  
Carbon Dioxide ◽  
Carbonic Anhydrase ◽  
Final Section ◽  
Carbon Dioxide Capture ◽  
Special Section ◽  
Atmospheric Temperature ◽  
Carbonic Anhydrases ◽  
The Past

In the past decade, the capture of anthropic carbonic dioxide and its storage or transformation have emerged as major tasks to achieve, in order to control the increasing atmospheric temperature of our planet. One possibility rests on the use of carbonic anhydrase enzymes, which have been long known to accelerate the hydration of neutral aqueous CO2 molecules to ionic bicarbonate species. In this paper, the principle underlying the use of these enzymes is summarized. Their main characteristics, including their structure and catalysis kinetics, are presented. A special section is next devoted to the main types of CO2 capture reactors under development, to possibly use these enzymes industrially. Finally, the possible application of carbonic anhydrases to directly store the captured CO2 as inert solid carbonates deserves a review presented in a final section.

Electropolymerized Carbonic Anhydrase Immobilization for Carbon Dioxide Capture

Langmuir ◽  
2014 ◽  
Vol 30 (23) ◽  
pp. 6915-6919 ◽  
Author(s):  
Geraldine Merle ◽  
Sylvie Fradette ◽  
Eric Madore ◽  
Jake E. Barralet
Keyword(s):  
Carbon Dioxide ◽  
Carbonic Anhydrase ◽  
Carbon Dioxide Capture
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