Characterization of immobilized glucose oxidase—catalase and their deactivation in a fluid-bed reactor |
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Authors: | Leman Tarhaqn Azmi Telefoncu |
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Institution: | (1) Department of Chemistry, Faculty of Education, Dokuz Eylüi University, 35150 Buca-ízmir, Turkey;(2) Department of Biochemistry, Faculty of Science, University of Ege, 35100 Bornova-ízmir, Turkey |
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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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Keywords: | Immobilization of GOD and CAT on the support immobilized GOD-CAT properties of immobilized GOD-CAT gluconic acid production with GOD-CAT deactivation of GOD and CAT by H2O2 |
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