An enzyme obtained from mycelia of fungi, such as Aspergilli and Penicillia; a typical aerobic dehydrogenase which catalyzes the oxidation of glucose to gluconic acid (molecular oxygen is reduced to hydrogen peroxide). It is a flavoprotein, the prosthetic group being flavine-adenine dinucleotide (FAD). Commercial prepns frequently contain appreciable amounts of another enzyme, catalase, which is desirable for certain uses since it removes hydrogen peroxide aerobically generated by glucose oxidase. Names of some commercial prepns are: DeeO, Fermcozyme, OxyBan, Ovazyme. Isoln from Penicillia cultures: Coulthard et al., Biochem. J. 39, 24 (1945). Commercial production from Aspergilli and Penicillia: Goldsmith et al., US 2926122 (1960); from Aspergillus niger: Faucett et al., US 3102081 (1963 to Miles Labs.). Removal of proteolytic enzymes from glucose oxidase (contg catalase) obtained from Aspergilli or Penicillia cultures: Ohlmeyer, US 2940904 (1960 to Ben L. Sarett). Separation from catalase: Pazur et al., Biochim. Biophys. Acta 65, 369 (1962). Properties: Muller, Enzymologia 10, 40 (1941); Keilin, Hartree, Biochem. J. 42, 221 (1948), 50, 331 (1952). Reviews: L. A. Underkofler “Glucose Oxidase: Production, Properties, Present and Potential Applications” in Soc. Chem. Ind. (London) Monograph no. 11, 72-86 (1961); R. Bentley, “Glucose Oxidase” in The Enzymes vol. 7, P. D. Boyer et al., Eds. (Academic Press, New York, 1963) pp 567-586. Review of use as analytical reagent: J. Raba, H. A. Mottola, Crit. Rev. Anal. Chem. 25, 1-42 (1995).