Leaders in monolith chromatography


Characterization of CIM Monoliths as Enzyme Reactors

M. Vodopivec, A. Podgornik, M. Berovič, A. Štrancar

Journal of Chromatography B, 795 (2003) 105-113

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 Km and the turnover number k3 of the immobilized enzymes were found to be flow-unaffected. Furthermore, the Km 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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