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Biocatalysts and Bioreactor Design
Enzymatic fragmentation of cation exchange membrane bound immunoglobulin G
Article first published online: 14 OCT 2010
DOI: 10.1002/btpr.501
Copyright © 2010 American Institute of Chemical Engineers (AIChE)
Additional Information
How to Cite
Yu, D. and Ghosh, R. (2011), Enzymatic fragmentation of cation exchange membrane bound immunoglobulin G. Biotechnol Progress, 27: 61–66. doi: 10.1002/btpr.501
Publication History
- Issue published online: 10 FEB 2011
- Article first published online: 14 OCT 2010
- Accepted manuscript online: 25 AUG 2010 09:25AM EST
- Manuscript Revised: 15 JUN 2010
- Manuscript Received: 15 FEB 2010
Funded by
- Natural Science and Engineering Research Council (NSERC) of Canada
- Abstract
- Article
- References
- Cited By
Keywords:
- membrane bioreactor;
- enzyme;
- fragmentation;
- purification
Abstract
Immunoglobulin G (IgG) was immobilized on a stack of microporous cation-exchange membranes and pulsed with pepsin solution. Fc fragment and its sub-fragments thus produced were removed along with the reaction flow-through, whereas F(ab′)2 which remained membrane bound could subsequently be eluted in a pure form using salt. The extent of IgG fragmentation and the apparent reaction rate constant were both significantly higher than in equivalent liquid phase reaction, presumably due to a combination of mass transport, steric, and substrate concentration effects. This approach of using a membrane surface as molecule cutting board could be attractive in niche applications such as integrated enzymatic reaction and purification processes involving macromolecular substrates. © 2010 American Institute of Chemical Engineers Biotechnol. Prog., 2011