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CO2 hydration by immobilized carbonic anhydrase.
Sumana Bhattacharya1, Marc Schiavone, Subhra Chakrabarti
1ABRD Company LLC, 1555 Wood Road, Cleveland, OH 44121, USA. bhattas@ccf.org
Biotechnology and Applied Biochemistry
|May 30, 2003
Summary
Immobilizing carbonic anhydrase (CA) enzymes on inert matrices enhances their stability and reusability. This innovation supports CO2 concentration for improved Rubisco activity in bioreactors.
Area of Science:
- Biochemistry
- Enzyme Engineering
- Biotechnology
Background:
- Carbonic anhydrase (CA) is crucial for CO2 hydration.
- Efficient CO2 capture is vital for biotechnological applications like Rubisco-catalyzed carbon fixation.
- Enzyme immobilization can improve enzyme stability and performance.
Purpose of the Study:
- To immobilize bovine and human carbonic anhydrase (isoform II) using covalent coupling methods.
- To evaluate the activity, stability, and reusability of immobilized CA.
- To assess the potential of immobilized CA for CO2 concentration in bioreactors.
Main Methods:
- Covalent coupling of carbonic anhydrase (isoform II) from bovine and human erythrocytes to inert matrices.
- Determination of enzyme activity via CO2 hydration assays.
- Evaluation of immobilized enzyme stability under varying operational conditions and storage.
- Assessment of enzyme reusability.
Main Results:
- Immobilization of carbonic anhydrase was achieved using different covalent coupling techniques.
- Immobilized carbonic anhydrase exhibited enhanced thermal and storage stability compared to soluble enzyme.
- Reusability of the immobilized enzyme was significantly improved.
- The study confirmed the potential of immobilized CA for CO2 concentration.
Conclusions:
- Enzyme immobilization using covalent coupling enhances the stability and reusability of carbonic anhydrase (isoform II).
- Immobilized carbonic anhydrase shows promise for applications requiring efficient CO2 concentration, such as in bioreactors for Rubisco-catalyzed fixation.