Purification and Properties of the Glucose Oxidase from Aspergillus Niger.

Glucose oxidase (/3-n-glucose : 02 oxidoreductase, EC 1.1.3.4) has been highly purified from the extracts of three fungi, Penicillium not&urn (1, 2), Penicillium amagasakiense (3, 4), and Aspergillus niger (5, 6). It has also been identified and sometimes partially purified from a number of other sources. Some of these sources are reviewed by Schepartz and Subers (7). Recently Pazur and Kleppe (6) have studied the specificity, and Gibson, Swoboda, and Massey (8, 9), the kinetics and mode of action, of the glucose oxidase from A. niger. Pazur, Kleppe, and Ball (10) have made the interesting discovery that this enzyme is a glycoprotein. It has generally been assumed that the glucose oxidases from different sources have the same properties. In this paper some of the physical and chemiral properties of t)he enzyme purified from A. niger are examined and compared with published data for glucose oxidases from other fungal sources. It is felt that the properties of the glucose oxidases isolated from P. not&urn (2, 11) and P. amagusakiense (4, 12) are sufficiently different from those of the il. niger enzyme to warrant more detailed intercomparison in the future.