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The glucose oxidase enzyme (GOx or GOD) also known as notatin (EC number 1.1.3.4) is an oxidoreductase that catalyses the oxidation of glucose to hydrogen peroxide and D-glucono-δ-lactone. This enzyme is produced by certain species of fungi and insects and displays antibacterial activity when oxygen and glucose are present.
An important example is EC 7.1.1.9 cytochrome c oxidase, the key enzyme that allows the body to employ oxygen in the generation of energy and the final component of the electron transfer chain. Other examples are: EC 1.1.3.4 Glucose oxidase; EC 1.4.3.4 Monoamine oxidase; EC 1.14.-.- Cytochrome P450 oxidase; EC 1.6.3.1 NADPH oxidase
A colorless solid, it is an oxidized derivative of glucose. It is typically produced by the aerobic oxidation of glucose in the presence of the enzyme glucose oxidase. The conversion cogenerates hydrogen peroxide, which is often the key product of the enzyme: C 6 H 12 O 6 + O 2 → C 6 H 10 O 6 + H 2 O 2
The glucose-methanol-choline (GMC) oxidoreductases are FAD flavoproteins oxidoreductases. [1] [2] These enzymes include a variety of proteins; choline dehydrogenase (CHD) EC 1.1.99.1, methanol oxidase (MOX) EC 1.1.3.13 and cellobiose dehydrogenase EC 1.1.99.18 [3] which share a number of regions of sequence similarities.
Now, however, the membrane is impregnated with immobilized glucose oxidase (GOx). [7] The GOx will consume some of the oxygen as it diffuses towards the PT electrode, incorporating it into H 2 O 2 and gluconic acid. [3] The rate of reaction current is limited by the diffusion of both glucose and oxygen.
In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor.
Many glucose meters employ the oxidation of glucose to gluconolactone catalyzed by glucose oxidase (sometimes known as GOx). Others use a similar reaction catalysed instead by another enzyme, glucose dehydrogenase (GDH). This has the advantage of sensitivity over glucose oxidase but is more susceptible to interfering reactions with other ...
The extreme discrepancy of the catalytic efficiencies of P. chrysosporium CDH for cellobiose over glucose (87500 : 1) is being connected to the physiological role of the white-rot basidiomycete enzyme. [18] In ascomycete CDHs the discrimination of glucose is less strict [19] and a wider spectrum of mono- and oligosaccharides are converted. Of ...