Hydroxides of magnesium and zinc, aluminum oxide, zinc phosphate, and co-precipitated Ca3(PO4)2 and Mg(OH)2 were efficient in binding extracellular glucose oxidase (GO) of P. adametzii LF F-2044.1 in a culture liquid filtrate (CLF). Basic Al2O3 was the most appropriate adsorbent for GO isolation from the CLF of the fungus. A GO isolation method was developed, which allowed for obtaining an enzyme with a high degree of purification. Spectral properties of the enzyme, its catalytic activity, and stability were characterized. The GO of P. adametzii LF F-2044.1 exhibited high pH stability, retaining activity within the range 4.5–9.0. The rate that GO-catalyzed D-glucose oxidation increased as the temperature increased (up to approximately 60°C). The catalytic activity and thermal stability of GO depended on its concentration in the medium. Under optimum conditions, the fractions GO-1 and GO-2 were characterized by K M values of 1.56 × 10−2 and 2.19 × 10−2 M, respectively; the corresponding values of k cat equaled 235.1 and 318.2 s−1.