Optimization and Immobilization of Glucose Oxidase on Gum Tragacanth Carrier

Glucose oxidase (β-D-glucose: oxygen-oxidoreductase, EC 1.1.3.4) from Aspergillus niger, is a flavoprotein which catalyses the oxidation of β-D-glucose to D-δ glucono-lactone, which subsequently hydrolyzes spontaneously to gluconic acid using molecular oxygen as the electron acceptor. Apart from being an analytical tool in biosensors for medical applications and environmental monitoring glucose oxidase (GOD) finds application in food and fermentation industry. In this study, glucose oxidase (GOD) was encapsulated within tragacanth gel capsules and the optimal conditions for immobilized GOD were obtained. Glucose oxidase was immobilized on gum tragacanth carrier with Microencapsulation method and the effects of pH, temperature, oxygen, concentrations of substrate (glucose) were studied and the optimal conditions for immobilized GOD were obtained. The enzyme activity was measured through pH- control. The optimal conditions for immobilized enzyme were: T= 36 °C, pH= 6, glucose concentration 0.1 M and the oxygen flow rate = 1 L/min. In optimum condition the activity of immobilized enzyme is preserved up to 75% after 8 repeated uses. As the results are shown gum tragacanth is a proper and economic biopolymer that might be used for immobilization.