- Title
- A study of bovine and human carbonic anhydrases as a model enzyme system for CO₂ hydration in post combustion capture
- Creator
- Phan, Duong T.; Burns, Robert C.; Puxty, Graeme; Williams, Michelle; Haritos, Victoria S.; Maeder, Marcel
- Relation
- International Journal of Greenhouse Gas Control Vol. 37, p. 85-89
- Publisher Link
- http://dx.doi.org/10.1016/j.ijggc.2015.03.016
- Publisher
- Elsevier
- Resource Type
- journal article
- Date
- 2015
- Description
- The Post Combustion Capture (PCC) process is currently the most applicable and effective approach to reduce emissions of CO₂ from fossil fuel electricity generation. If the rate of CO₂ hydration can be accelerated, the size of the absorber column can be reduced accordingly. Carbonic anhydrase type II (CAII), being one of the most active enzymes known for the reaction of CO₂ with H₂O, is a promising catalyst for CO₂ absorption in aqueous solution for PCC application. In this study, the catalytic efficiencies of human (hCAII), wild type bovine (wtbCAII), and a series of wtbCAIIs (bCAM1-bCAM9) structurally modified in an attempt to improve thermal and salt stability were determined by stopped-flow spectrophotometry at 25°C. wtbCAII and hCAII were found to have the highest activity for the hydration of CO2 while bCAM9 was the least efficient catalyst (catalytic rate constants of 1.198(6)×10⁸, 1.14(1)×10⁸ and 0.77(2)×10⁸M⁻¹s⁻¹, respectively). The remaining mutants have similar catalytic efficiencies for CO₂ hydration and fall in the range of 8.63(6)×10⁷-1.072(2)×10⁸M⁻¹s⁻¹. In addition to these results, this study also verifies the analytical method developed for the study of enzymatic systems.
- Subject
- carbonic anhydrases; bovine; human; catalytic efficiency; post combustion capture; CO₂ capture
- Identifier
- http://hdl.handle.net/1959.13/1323258
- Identifier
- uon:24765
- Identifier
- ISSN:1750-5836
- Language
- eng
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