Glukosoxidas

Glukosoxidas, more commonly known as glucose oxidase (GOx), is an enzyme that catalyzes the oxidation of β-D-glucose to glucono-δ-lactone with the concurrent reduction of molecular oxygen to hydrogen peroxide. It is a flavoprotein containing the cofactor flavin adenine dinucleotide (FAD) and is classified as an oxidoreductase (EC 1.1.3.4). The lactone produced rapidly hydrolyzes in water to gluconic acid. In typical applications, molecular oxygen serves as the electron acceptor, although alternative systems can be used in engineered setups.

The enzyme is predominantly sourced from fungi, with Aspergillus niger and Penicillium species historically providing commercial GOx. It is usually a homodimer, and each subunit contains one FAD cofactor. GOx shows high specificity for β-D-glucose, making it valuable for quantitative glucose determination in various contexts.

Applications of glucose oxidase are widespread. In clinical chemistry and biotechnology, it is used in blood glucose sensing and enzymatic assays due to its ability to generate hydrogen peroxide proportional to glucose concentration. In biosensors, GOx is often immobilized on electrode surfaces, translating glucose levels into electrical signals through amperometric or mediated detection of the produced hydrogen peroxide or by coupling with a peroxidase system in colorimetric assays. In the food and packaging industries, GOx is used to remove dissolved oxygen, helping to preserve color, flavor, and shelf life by reducing oxidative spoilage.

Safety and handling follow standard practices for enzymatic preparations. Glucose oxidase is valued for its specificity, reliability, and versatility across diagnostic, analytical, and industrial applications.