Modified Enzyme Removes CO2 , With Stability and Longevity in Bioreactors and Dialysis Machines
These modified carbonic anhydrase enzymes maximize sequestration of carbon dioxide in industrial and biomedical processes. Global warming, has increased the demand for CO2 sequestration and biofuel/biomass production in recent years. Current use of carbonic anhydrase in industrial applications is limited by the relative instability of the enzyme in harsh environments, resulting in decreased cost-efficiency and productivity. Through engineering methods targeting specific sets of amino acids, University of Florida researchers have created an enzyme with improved stability, longevity, and tolerance to moderately acidic pH, augmenting the catalysis of CO2 to bicarbonate.
Modified carbonic anhydrase enzyme improves CO2 sequestration in industrial and biomedical applications
- Design of modified carbonic anhydrase enzyme based on the structure of the human enzyme, maximizing reactivity in biomedical applications
- Increases overall rate of catalysis and CO2 to bicarbonate conversion, improving efficiency of carbonic anhydrase in CO2 sequestration
- Better stability, longevity, and tolerance to acidic pH, augmenting effectiveness of enzymes even in adverse conditions
Carbonic anhydrase is used in CO2 sequestration and industrial applications. However, harsh environments can make the enzyme unstable. Researchers at the University of Florida have discovered engineering methods to improve the stability and catalysis for CO2 sequestration by altering and replacing amino acids in the enzyme. By using known information from carbonic anhydrase structures, a small set of targeted amino acids are changed, which improve the stability, longevity, and tolerance of the enzymes. In addition, the replacement of amino acids increases the catalytic rate of CO2 hydration and HCO3 dehydration in some cases.