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Immobilization of several multienzyme systems on porous glass beads

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Abstract

Equimolar concentrations of malate dehydrogenase (EC 1.1.1.37) and fumarase (EC 4.2.1.2) and equimolar concentrations of malate dehydrogenase and citrate synthase (EC 4.1.3.7) were simultaneously immobilized to alkylamine porous silica beads with gluteraldehyde. The activity of each enzyme in the two-enzyme immobilized systems was determined and exact concentrations of the free nonimmobilized enzymes were prepared. The activities of the coupled free and coupled immobilized systems were measured, and it was observed that there was a 10-fold enhancement in the catalysis of the immobilized enzymes.

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Abbreviations

NAD+ :

nicotinamideadenine dinucleotide

NADH:

reduced form of NAD+

DTNB:

dithiobis (2-nitrobenzoic acid)

CoA:

coenzyme A

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Authors and Affiliations

  1. Chemistry Department, Auburn University, 36830, Auburn, Alabama

    Phillip M. Heidepriem, Herbert H. Kohl & Michael E. Riedman

Authors
  1. Phillip M. Heidepriem
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  2. Herbert H. Kohl
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  3. Michael E. Riedman
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Heidepriem, P.M., Kohl, H.H. & Riedman, M.E. Immobilization of several multienzyme systems on porous glass beads. Journal of Solid-Phase Biochemistry 5, 5–9 (1980). https://doi.org/10.1007/BF02991898

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  • DOI: https://doi.org/10.1007/BF02991898

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