Glucose Oxidase-dextran Conjugates with Enhanced Stabilities Against Temperature and pH |
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| Authors: | Melda Altikatoglu Yeliz Basaran Candan Arioz Ayse Ogan Huriye Kuzu |
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| Institution: | (1) Department of Chemistry, Faculty of Sciences and Letters, Yildiz Technical University, Davutpasa Campus, Esenler, 34210 Istanbul, Turkey;(2) Department of Bioengineering, Faculty of Chemical and Metallurgical Engineering, Yildiz Technical University, Davutpasa Campus, Esenler, 34210 Istanbul, Turkey;(3) Department of Chemistry, Faculty of Sciences and Letters, Marmara University, Goztepe, 34722 Istanbul, Turkey |
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| Abstract: | Multipoint covalent bonding of glucose oxidase (EC 1.1.3.4) to hydrophilic natural polymer dextran and optimization of procedures
to obtain, with enhanced temperature and pH stabilities, were studied. Purified enzyme was conjugated with various molecular
weight dextrans (17.5, 75, and188 kD) in a ratio of 20:1, 10:1, 1:1, 1:5, 1:10, 1:15, and 1:20. After 1 h of incubation at
pH 7, the activities of purified enzyme and conjugates were determined at different temperatures (25°C, 30°C, 35°C, 40°C,
50°C, 60°C, 70°C, and 80°C), and the results were evaluated for thermal resistance. Increases in temperature from 25°C to
50°C did not change the activities of the conjugates. The conjugate, which was prepared with 75 kDa dextran in a molar ratio
of 1:5, showed the highest thermal resistance and even the activity still remains at 80°C at pH 7.0. This conjugate also displayed
activity in a wide pH range (pH 4.0–7.0) at high temperatures. Conjugate, which was synthesized with 75 kDa dextran in a molar
ratio of 1:5, appears to be feasible and useful for biotechnological applications. |
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