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Immobilization of fumarase and malate dehydrogenase on agarose efficiency of activity as a function of the enzyme ratio

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Abstract

Two enzymes, L-malate dehydrogenase, L-malate: NAD+ oxidoreductase (EC 1.1.1.37) and fumarase, L-malate hydrolyase (EC 4.2.1.2) were immobilized on a (Sepharose 4B) resin by the cyanogen bromide method. Studies showed that the matrix-immobilized fumarase retains the same characteristics as the free enzyme, while the matrix-immobilized malate dehydrogenase has reduced activity. The activity of the coupled enzymes is more enzymeconcentration dependent than the free enzymes, and at a ratio of 0.3 (fumarase: malate dehydrogenase) the simultaneously coupled immobilized enzymes become a better catalytic system. Individually immobilized enzymes, mixed to form a coupled system, yielded the poorest catalytic action.

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Authors and Affiliations

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

    Nilgun Erekin & Michael E. Friedman

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  1. Nilgun Erekin
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  2. Michael E. Friedman
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This research was supproted by a NSF-URP grant, No. SM176-83486

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Erekin, N., Friedman, M.E. Immobilization of fumarase and malate dehydrogenase on agarose efficiency of activity as a function of the enzyme ratio. Journal of Solid Phase Biochemistry 4, 123–130 (1979). https://doi.org/10.1007/BF02991866

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  • DOI: https://doi.org/10.1007/BF02991866

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