CO2 hydration by immobilized carbonic anhydrase

Sumana Bhattacharya; Marc Schiavone; Subhra Chakrabarti; Sanjoy K. Bhattacharya

doi:10.1042/BA20030060

CO₂ hydration by immobilized carbonic anhydrase

Sumana Bhattacharya, Marc Schiavone, Subhra Chakrabarti, Sanjoy K. Bhattacharya

Research output: Contribution to journal › Article › peer-review

55 Scopus citations

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)
Pages (from-to)	111-117
Number of pages	7
Journal	Biotechnology and Applied Biochemistry
Volume	38
Issue number	2
DOIs	https://doi.org/10.1042/BA20030060
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

Access to Document

10.1042/BA20030060

Cite this

@article{d579c1f132ed4a108ebfee521034c896,

title = "CO2 hydration by immobilized carbonic anhydrase",

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.",

keywords = "Carbonic anhydrase, CO concentration, CO-fixation bioprocess, Immobilized carbonic anhydrase, Immobilized carbonic anhydrase bioreactor",

author = "Sumana Bhattacharya and Marc Schiavone and Subhra Chakrabarti and Bhattacharya, {Sanjoy K.}",

year = "2003",

month = oct,

day = "1",

doi = "10.1042/BA20030060",

language = "English (US)",

volume = "38",

pages = "111--117",

journal = "Journal of Applied Biochemistry",

issn = "0885-4513",

publisher = "Wiley-Blackwell",

number = "2",

}

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 - Journal of Applied Biochemistry

JF - Journal of Applied Biochemistry

SN - 0885-4513

IS - 2

ER -