Biocatalytic reactors based on ribonuclease A immobilized on macroporous monolithic supports

Immobilized enzyme reactors (IMERs) produced by the covalent attachment of ribonuclease A to macroporous methacrylate-based monolithic supports using different experimental approaches are discussed and compared. Enzyme immobilization was carried out by direct covalent binding, as well as through att...

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Bibliographic Details
Published in:Analytical and bioanalytical chemistry 2013-03, Vol.405 (7), p.2195-2206
Main Authors: Ponomareva, E. A., Volokitina, M. V., Vinokhodov, D. O., Vlakh, E. G., Tennikova, T. B.
Format: Article
Language:English
Subjects:
Analytical Chemistry
Animals
Attachment
Binding
Biocatalysis
Biochemistry
Catalysts
Cattle
Characterization and Evaluation of Materials
Chemical bonds
Chemical properties
Chemical reaction, Rate of
Chemistry
Chemistry and Materials Science
Composition
Covalence
Efficiency
Enzymes
Enzymes, Immobilized - chemistry
Flow rates
Food Science
Kinetics
Laboratory Medicine
Mathematical analysis
Monitoring/Environmental Analysis
Original Paper
Polymers
Porosity
Production processes
Proteins
Proteomics
Reactors
Resins, Synthetic - chemistry
Ribonuclease A
Ribonuclease, Pancreatic - chemistry
Spacers
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Summary:Immobilized enzyme reactors (IMERs) produced by the covalent attachment of ribonuclease A to macroporous methacrylate-based monolithic supports using different experimental approaches are discussed and compared. Enzyme immobilization was carried out by direct covalent binding, as well as through attachment via a polymer spacer. The kinetic properties of an IMER operating in either recirculation mode or zonal elution mode were studied. Additionally, the effect of flow rate on the bioconversion efficiency of each IMER sample was examined. Figure Enzyme immobilization via aldehyde-bearing macromolecular spacer on the surface of epoxy-containing monoliths
ISSN:1618-2642
1618-2650
DOI:10.1007/s00216-012-6391-y