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Characterization of CIM monoliths as enzyme reactors.

Authors
  • Vodopivec, Martina
  • Podgornik, Ales
  • Berovic, Marin
  • Strancar, Ales
Type
Published Article
Journal
Journal of Chromatography B
Publisher
Elsevier
Publication Date
Sep 25, 2003
Volume
795
Issue
1
Pages
105–113
Identifiers
PMID: 12957174
Source
Medline
License
Unknown

Abstract

The immobilization of the enzymes citrate lyase, malate dehydrogenase, isocitrate dehydrogenase and lactate dehydrogenase to CIM monolithic supports was performed. The long-term stability, reproducibility, and linear response range of the immobilized enzyme reactors were investigated along with the determination of the kinetic behavior of the enzymes immobilized on the CIM monoliths. The Michaelis-Menten constant K(m) and the turnover number k(3) of the immobilized enzymes were found to be flow-unaffected. Furthermore, the K(m) values of the soluble and immobilized enzyme were found to be comparable. Both facts indicate the absence of a diffusional limitation in immobilized CIM enzyme reactors.

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