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 |
|---|---|
| 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 |
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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
Cite this
CO2 hydration by immobilized carbonic anhydrase. / Bhattacharya, Sumana; Schiavone, Marc; Chakrabarti, Subhra; Bhattacharya, Sanjoy K.
In: Biotechnology and Applied Biochemistry, Vol. 38, No. 2, 01.10.2003, p. 111-117.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - CO2 hydration by immobilized carbonic anhydrase
AU - Bhattacharya, Sumana
AU - Schiavone, Marc
AU - Chakrabarti, Subhra
AU - Bhattacharya, Sanjoy K
PY - 2003/10/1
Y1 - 2003/10/1
N2 - 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.
AB - 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.
KW - Carbonic anhydrase
KW - CO concentration
KW - CO-fixation bioprocess
KW - Immobilized carbonic anhydrase
KW - Immobilized carbonic anhydrase bioreactor
UR - http://www.scopus.com/inward/record.url?scp=0142042513&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0142042513&partnerID=8YFLogxK
U2 - 10.1042/BA20030060
DO - 10.1042/BA20030060
M3 - Article
C2 - 12773097
AN - SCOPUS:0142042513
VL - 38
SP - 111
EP - 117
JO - Biotechnology and Applied Biochemistry
JF - Biotechnology and Applied Biochemistry
SN - 0885-4513
IS - 2
ER -