Production, purification, and characterization of a fusion protein of carbonic anhydrase from Neisseria gonorrhoeae and cellulose binding domain from Clostridium thermocellum thermocellum

  • Liu Z
  • Bartlow P
  • Dilmore R
 et al. 
  • 13

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Abstract

Carbon dioxide capture technologies have the potential to become an important climate change mitigation option through sequestration of gaseous CO2. A new concept for CO2 capture involves use of immobilized carbonic anhydrase (CA) that catalyzes the reversible hydration of CO2 to HCO3? and Hþ. Cost-efficient production of the enzyme and an inex- pensive immobilization system are critical for development of economically feasible CA- based CO2 capture processes. An artificial, bifunctional enzyme containing CA from Neisse- ria gonorrhoeae and a cellulose binding domain (CBD) from Clostridium thermocellum was constructed with a His6 tag. The chimeric enzyme exhibited both CA activity and CBD bind- ing affinity. This fusion enzyme is of particular interest due to its binding affinity for cellu- lose and retained CA activity, which could serve as the basis for improved technology to capture CO2 from flue gasses.

Author-supplied keywords

  • carbon dioxide hydration
  • carbonic anhydrase
  • cellulose binding domain

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Authors

  • Zhu Liu

  • Patrick Bartlow

  • Robert M Dilmore

  • Yee Song

  • Zhiwei Pan

  • Richard Koepsel

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