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Results 1 - 10 of 15 > >>
EC Number Application Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.9analysis a photoelectrochemical biosensor for quantitative detection of galactose is obtained immobilizing galactose oxidase on TiO2 nanorod arrays modified F-doped tin oxide (FTO) electrode. The direct electron transfer to galactose oxidase is achieved. The generated photocurrent of the stable platform is significantly enhanced after the addition of galactose in solution and the photocurrent intensity shows linear relationship with the galactose concentration. CaCl2, uric acid and ascorbic acid have no interference with the detection of galactose. The sensor can be reused and applied to measure the concentration of galactose in lactose-free milk 763383
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.9analysis galactose oxidase adsorbed on, and covalently bound to, silica carriers is used for analytical determinations of D-galactose and galactose-containing sugars. Using a flowing oxygen electrode of the Clark-type, sensor system for enzymatic analysis of water solutions of galactose-containing carbohydrates is made. Measurements are taken both in the pulse and continuous modes of a substrate flowing through a column with an immobilized biocatalyst -, 684425
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.9analysis galactose oxidase is an important component in electrochemical biosensors of galactose that are used for various biotechnology applications 742748
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.9analysis the enzyme can be useful in biosensors 743101
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.9biotechnology technology: creating hybrid-system by immobilization of GOase on gold electrode, technology enables creation of biosensors and biofuel cells and studying electrochemically the catalytic mechanism of reactions for which free radicals and electron-transfer reactions are involved 698480
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.9degradation the enzyme can be used for oxygen removal 743101
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.9diagnostics determination of galactose or lactose concentration in complex biological fluids by immobilized galactose oxidase 389876
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.9energy production the enzyme is useful in fuel cells and the usage of biofuel cell with glucose 743101
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.9molecular biology glycoprotein labeling using engineered variants of galactose oxidase, overview 725202
Display the word mapDisplay the reaction diagram Show all sequences 1.1.3.9synthesis combination of UDP-Glc(NAc) 4'-epimerase and galactose oxidase in a one-pot synthesis of biotinylated nucleotide sugars. The enzymatic epimerization of uridine 5’-diphospho-alpha-D-glucose and uridine 5’-diphospho-N-acetyl-alpha-D-glucosamine and the subsequent oxidation of uridine 5’-diphospho-alpha-D-galactose and uridine 5’-diphospho-N-acetyl-alpha-D-galactosamine are combined with chemical biotinylation with biotin-epsilon-amidocaproylhydrazide in a one-pot synthesis. A mixture (1.0:1.4) of the biotinylated nucleotide sugars uridine 5’-diphospho-6-biotin-epsilon-amidocaproylhydrazino-alpha-D-galactose and uridine 5’-diphospho-6-biotin-epsilon-amidocaproylhydrazino-alpha-D-glucose, is produced in a reaction started with uridine 5’-diphospho-alpha-D-glucose. One product, uridine 5’-diphospho-6-biotin-epsilon-amidocaproylhydrazino-N-acetyl-alpha-D-galactosamine is formed when the reaction is initiated with uridine 5’-diphospho-N-acetyl-alpha-D-glucosamine 684251
Results 1 - 10 of 15 > >>