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- W1736387639 abstract "Glucose oxidase, an important source of hydrogen peroxide in lignin-degrading cultures of Phanerochaete chrysosporium, was purified to electrophoretic homogeneity by a combination of ion-exchange and molecular sieve chromatography. The enzyme is a flavoprotein with an apparent native molecular weight of 180,000 and a denatured molecular weight of 80,000. This enzyme does not appear to be a glycoprotein. It gives optimal activity with D-glucose, which is stoichiometrically oxidized to D-gluconate. The enzyme has a relatively broad pH optimum of 4 to 5. It is inhibited by Ag+ (10 mM) and o-phthalate (100 mM), but not by Cu2+, NaF, or KCN (each 10 mM)." @default.
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- W1736387639 date "1986-04-01" @default.
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- W1736387639 title "Purification and characterization of glucose oxidase from ligninolytic cultures of Phanerochaete chrysosporium" @default.
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- W1736387639 doi "https://doi.org/10.1128/jb.166.1.269-274.1986" @default.
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