Abstract
AbstractThe kinetics of oxidation of glucose solution by dissolved oxygen in the presence of glucose oxidase and excess catalase were studied both theoretically and experimentally. The kinetic model used was based on the detailed mechanism of the reaction. The description of the model is given by the Michaelis–Menten equation for the case of two substrates. The experiments were carried out in a closed reactor at a temperature of 25°C and pH 5.55. Commercial enzymes were used. Kinetic constants of the reaction were evaluated by fitting the oxygen concentration profiles calculated from the model to those found experimentally, by the method of nonlinear regression. The rate of D‐glucose mutarotation to α and β form, and distortion of data caused by the dynamics of the applied oxygen probe were taken into account. The determined kinetic constants of the reactions are in good agreement with those given in the literature for purified enzymes. Adoption of literature kinetic data of this reaction to the determination of aeration capacity of fermentors by means of glucose oxidase systems has proved possible.
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