Abstract
The enzyme carbonic anhydrase (isoform II) from bovine and human erythrocytes was immobilized using different covalent coupling methods on inert matrices. Immobilized carbonic anhydrase may enable concentration of CO 2 for Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase)- catalysed fixation in bioreactors. In the present study the activity of carbonic anhydrase with respect to hydration of CO2 using soluble and immobilized enzymes was determined. The stability of the immobilization matrix, the properties of the immobilized enzymes subjected to a variation in operation variables and the activity profile with respect to storage are reported. Immobilization imparted greater thermal and storage stability and enhanced reusability.
Original language | English (US) |
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Pages (from-to) | 111-117 |
Number of pages | 7 |
Journal | Biotechnology and Applied Biochemistry |
Volume | 38 |
Issue number | 2 |
DOIs | |
State | Published - Oct 1 2003 |
Externally published | Yes |
Keywords
- Carbonic anhydrase
- CO concentration
- CO-fixation bioprocess
- Immobilized carbonic anhydrase
- Immobilized carbonic anhydrase bioreactor
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Biotechnology