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Immobilization of ß-Galactosidase on Benzoquinone-Activated Bead-Cellulose1

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Abstract

ß-galactosidase from Escherichia coli was immobilized on porous bead cellulose by a benzoquinone coupling method. Optimum conditions for activation and coupling were investigated, and the kinetic parameters of the immobilized enzyme described. The binding capacity was 15.6mg/g of wet conjugate, corresponding to 109 mg/g dry matrix. A saturation activity of 4100 U/g dry cellulose beads was achieved. The apparent Michaelis constant of the immobilized ß-galactosidase at pH 7.6 for orthonitrophenylgalactopyranoside was 2.4 x 10-3 mol/liter, as compared to 2.4 x 10-4 mol/liter of the native enzyme. The stability of benzoquinone-activated bead cellulose and of immobilized ß galactosidase were also determined.

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Authors and Affiliations

  1. Institut für Biochemie und Endokrinologie, FB 18 Justus-Liebig- Universität Giessen, D-6300, Giessen, Federal Republic of Germany

    Moonjin Chun, Gisela Dickopp & Manfred Sernetz

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  1. Moonjin Chun
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  2. Gisela Dickopp
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  3. Manfred Sernetz
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Chun, M., Dickopp, G. & Sernetz, M. Immobilization of ß-Galactosidase on Benzoquinone-Activated Bead-Cellulose1. Journal of Solid-Phase Biochemistry 5, 211–221 (1980). https://doi.org/10.1007/BF03000657

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  • DOI: https://doi.org/10.1007/BF03000657

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