The advent in climate awareness has sparked an effort to develop novel and practical ways to reduce greenhouse gas (GHG) emissions produced during industrial processes. Mainly, there is a strong effort to sequester CO2, one of the most abundant GHG that is produced as a byproduct in industrial applications. However, the removal of CO2 is often costly and requires harsh chemical processes, thus limiting the practicality of employing these technologies into industrial use. As a solution to the current issues with industrial CO­2 sequestration, the enzyme carbonic anhydrase (CA) has been utilized. CA catalyzes CO2 to bicarbonate and a proton by way of a double-displacement mechanism. As such, industrial removal of bicarbonate has shown to be a less costly and a more efficient process than CO2, thus making this reaction an extraordinary viable way to reduce atmospheric CO2 levels. Human CA isoform II is the most efficient CA known that shows a relatively high thermostability with a melting temperature of ~58°C and remains active in a wide-range of pH values. However, for the enzyme to be used in industrial CO2 sequestration it must remain active at even higher temperatures and more extreme pH levels. Here we present structural and functional characterizations of several engineered variants of CA II and show that it is possible to modulate its thermo- and pH stability via modifications of key residues on the enzymes surface and in its active site. Our results show that CA can be used as a biomimetic CO2 sequestering agent.

Increasing thermo- and pH stability in carbonic anhydrase II for bioremediation purposes: A novel approach to industrial CO2 sequestration

249th National Meeting (2015)

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