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Biotechnology and Applied Biochemistry (2003) 38, (111–117) (Printed in Great Britain)

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CO₂ hydration by immobilized carbonic anhydrase

Sumana Bhattacharya*, Marc Schiavone*, Subhra Chakrabarti* and Sanjoy K. Bhattacharya†¹

*ABRD Company LLC, 1555 Wood Road, Cleveland, OH 44121, U.S.A., and †Department of Ophthalmic Research/I31, Cleveland Clinic Foundation, Cleveland, OH 44195, U.S.A.

Key words: carbonic anhydrase, CO₂ concentration, CO₂-fixation bioprocess, immobilized carbonic anhydrase, immobilized carbonic anhydrase bioreactor.

Abbreviations used: CA, carbonic anhydrase; CCM, CO₂-concentrating mechanism; C_i, inorganic carbon; Rubisco, ribulose-1,5-bisphosphate carboxylase/oxygenase; RuBP, D-ribulose 1,5-bisphosphate; WA unit, Wilbur–Anderson unit; DCC, dicarboxycarbodi-imide.

¹To whom correspondence should be addressed (e-mail bhattas@ccf.org).

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 CO₂ 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.

Received 8 April 2003/27 May 2003; accepted 29 May 2003

Published as Immediate Publication 29 May 2003, DOI 10.1042/BA20030060

© 2003 Portland Press Ltd