Pyranose Oxidase from Coriolus sp.

Pyranose oxidase (P2O), a homotetrameric protein consists of a covalently bound flavin adenine dinucleotide (FAD). It is seen mostly among wood-degrading basidiomycetes.

Pyranose Oxidase from Coriolus sp. has been used in the enzymatic oxidation of D-glucose (DG). It has also been used as a component in oxygen scavenging system (OSS) to increase the lifetime of the fluorophores.

Pyranose oxidase (P2O) can be used in clinical chemistry to determine 1,5-anhydro-d-glucitol marker, used for glycemic control in diabetes patients.

Pyranose oxidase (P2O) catalyzes the oxidation of aldopyranoses at position C-2 to yield the corresponding 2-ketoaldoses. The in vivo substrates of P2O are thought to be D-glucose, D-galactose, and D-xylose. They are oxidized to 2-keto-D-glucose (D-arabino-hexos-2-ulose, 2-dehydro-D-glucose), 2-keto-D-galactose (D-lyxo-hexos-2-ulose, 2-dehydro-D-galactose), and 2-keto-D-xylose (D-threopentos-2-ulose, 2-dehydro-D-xylose), respectively. Pyranose oxidase has significant activity with carbohydrates such as, L-sorbose, D-glucono-1,5-lactone, and D-allose. When pyranose oxidase catalyzes the oxidation of aldopyranoses, electrons are transferred to molecular oxygen which results in the formation of hydrogen peroxide.

Contains glutamate

One unit produces 1.0 μmol of hydrogen peroxide per minute at 37 °C, pH 7.0.