Activity and stability of immobilized carbonic anhydrase for promoting CO2 absorption into a carbonate solution for post-combustion CO2 capture

Bioresour Technol. 2011 Nov;102(22):10194-201. doi: 10.1016/j.biortech.2011.09.043. Epub 2011 Sep 17.

Abstract

An Integrated Vacuum Carbonate Absorption Process (IVCAP) currently under development could significantly reduce the energy consumed when capturing CO2 from the flue gases of coal-fired power plants. The biocatalyst carbonic anhydrase (CA) has been found to effectively promote the absorption of CO2 into the potassium carbonate solution that would be used in the IVCAP. Two CA enzymes were immobilized onto three selected support materials having different pore structures. The thermal stability of the immobilized CA enzymes was significantly greater than their free counterparts. For example, the immobilized enzymes retained at least 60% of their initial activities after 90 days at 50 °C compared to about 30% for their free counterparts under the same conditions. The immobilized CA also had significantly improved resistance to concentrations of sulfate (0.4 M), nitrate (0.05 M) and chloride (0.3 M) typically found in flue gas scrubbing liquids than their free counterparts.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Absorption
  • Animals
  • Biotechnology / methods*
  • Carbon Dioxide / metabolism*
  • Carbonates / metabolism*
  • Carbonic Anhydrases / metabolism*
  • Cattle
  • Enzyme Stability
  • Enzymes, Immobilized / metabolism*
  • Hydrolysis
  • Nitrophenols / metabolism
  • Porosity
  • Solutions
  • Temperature

Substances

  • Carbonates
  • Enzymes, Immobilized
  • Nitrophenols
  • Solutions
  • Carbon Dioxide
  • 4-nitrophenyl acetate
  • Carbonic Anhydrases