Glucose oxidase is a well-characterised flavoprotein that catalyses oxidation of β-D-Glucose at its first hydroxyl group, utilizing molecular oxygen as the electron acceptor, to produce D-glucono-delta-lactone and hydrogen peroxide. Glucose oxidase is a homodimeric enzyme, with an FAD molecule moncovalently but tightly bound at the active site of each 80 KDa subunit. The enzyme consists of two identical polypeptide chain subunits (80,000 Daltons) covalently linked by disulfide bonds. Each subunit contains one mole of Fe and one mole of FAD (flavin-adenine dinucleotide). The molecule consists of approximately 74% protein, 16% neutral sugar and 2% amino sugars. The FAD is replaceable with FHD (flavin-hypoxanthine dinucleotide) without loss of activity
Diagnostic application
Glucose oxidase can be utilized in the enzymatic determination of D-glucose in solution. As glucose oxidase oxidizes β-D-glucose to D-gluconolactate and hydrogen peroxide, horseradish peroxidase is often used as the coupling enzyme to visualize colorimetrically the formed hydrogen peroxide for the rapid determination of free glucose in samples. Enzymatic glucose biosensors use an electrode instead of O2 to take up the electrons needed to oxidize glucose and produce an electronic current in proportion to glucose concentration, which is the technology behind the disposable glucose sensor strips used by diabetics to monitor serum glucose levels.
Food industry applications
Glucose oxidase assay allows the monitoring of glucose levels in fermentation and bioreactors. It also helps food preservation by removing oxygen from food, wine, beer packaging and bottling. Glucose oxidase is widely used to remove residual glucose to inhibit non-enzymatic browning
Associated Targets
PYGMTchem Glycogen phosphorylase, muscle form 0 Activities
G2416299
