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Characterization of immobilized glucose oxidase—catalase and their deactivation in a fluid-bed reactor

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Abstract

2-Amino-4-chloro-s-triazine, a derivative of DEAE-cellulose, and acrolein/styrene copolymer were used as supports for the immobilization of glucose oxidase and catalase after being modified with diaminohexane followed by glutaraldehyde. Immobilization was carried out with optimum glucose oxidase-catalase ratios. The activity variations of the immobilized dual-enzyme systems were investigated in relation to pH and temperature. Time-dependent gluconic acid production resulting from the oxidation of glucose was monitored in a recycling fluid-bed reactor. The deactivation rates of glucose oxidase and catalase were investigated according to the first-order reaction kinetics depending on the presence of the intermediate product H2O2.

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Authors and Affiliations

  1. Department of Chemistry, Faculty of Education, Dokuz Eylüi University, 35150, Buca-Ízmir, Turkey

    Leman Tarhaqn & Azmi Telefoncu

  2. Department of Biochemistry, Faculty of Science, University of Ege, 35100, Bornova-Ízmir, Turkey

    Leman Tarhaqn & Azmi Telefoncu

Authors
  1. Leman Tarhaqn
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  2. Azmi Telefoncu
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Tarhaqn, L., Telefoncu, A. Characterization of immobilized glucose oxidase—catalase and their deactivation in a fluid-bed reactor. Appl Biochem Biotechnol 26, 45–57 (1990). https://doi.org/10.1007/BF02798392

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  • DOI: https://doi.org/10.1007/BF02798392

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