Function
Glucose oxidase catalyzes the oxidation of beta-D-glucose to D-glucono-delta-lactone and hydrogen peroxide in the presence of molecular oxygen. D-glucono-delta-lactone is sequentially hydrolyzed by lactonase to D-gluconic acid, and the resulting hydrogen peroxide is hydrolyzed by catalase to oxygen and water. The activity shows high specificity to beta-D-glucose, with very low to no activity towards L-glucose, 2-deoxy-D-glucose, 3-deoxy-D-glucose, 4-deoxy-D-glucose, 5-deoxy-D-glucose, 6-deoxy-D-glucose, 3-O-methyl-D-glucose, 4-O-methyl-D-glucose, 6-O-methyl-D-glucose, 4,6-O-benzylidene-D-glucose, 5-thio-5-deoxy-D-glucose, D-mannose, D-allose, D-galactose, D-fructose, D-arabinose, D-xylose, trehalose, melibiose, L-mannomethylose, lactose, sucrose or 1,5-anhydro-D-glucitol.
Biological Context
Subcellular Location: Secreted; Secreted, cell wall; Cytoplasm; Secreted, extracellular space, extracellular matrix
Product Specifications
Recombinant Aspergillus niger Glucose oxidase (gox), partial is a recombinant protein from Aspergillus niger, expressed in E.coli, covering amino acids 23-604aa, with N-terminal 10xHis-tagged tag, molecular weight 68.6kDa, purity Greater than 85% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications. Explore more Enzyme proteins →
