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Extracellular Glucose Oxidase of Penicillium funiculosum 46.1

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Abstract

A method for isolating extracellular glucose oxidase from the fungus Penicillium funiculosum 46.1 using ultrafiltration membranes was developed. Two samples of the enzyme with a specific activity of 914–956 IU were obtained. The enzyme exhibited a high catalytic activity at pH above 6.0. The effective rate constant of glucose oxidase inactivation at pH 2.6 and 16°C was 2.74 × 10–6 s–1. This constant decreased significantly as the pH of the medium increased (4.0–10.0). The temperature optimum for glucose oxidase–catalyzed β-D-glucose oxidation was in the range 30–65°C. At temperatures below 30°C, the activation energy for β-D-glucose oxidation was 6.42 kcal/mol; at higher temperatures, this parameter was equal to 0.61 kcal/mol. Kinetic parameters of glucose oxidase–catalyzed β-D-glucose oxidation depended on the initial concentration of the enzyme in the solution. Glucose oxidase also catalyzed the oxidation of 2-deoxy-D-glucose, maltose, and galactose.

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Authors and Affiliations

  1. National Academy of Sciences of Belarus, Institute of Microbiology, Minsk, 220141, Belarus

    T. V. Semashko & R. V. Mikhailova

  2. National Academy of Sciences of Belarus, Institute of Bioorganic Chemistry, Minsk, 220141, Belarus

    A. N. Eremin

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  1. T. V. Semashko
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  2. R. V. Mikhailova
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  3. A. N. Eremin
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Semashko, T.V., Mikhailova, R.V. & Eremin, A.N. Extracellular Glucose Oxidase of Penicillium funiculosum 46.1. Applied Biochemistry and Microbiology 39, 368–374 (2003). https://doi.org/10.1023/A:1024512316571

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