Alcohol Oxidase from Candida boidinii

Research area: Cell Signaling

Alcohol Oxidase (AOX) is a homo-octamer composed of eight flavin adenine dinucleotide (FAD) cofactors and belongs to the glucose-methanol-choline (GMC) family of oxidoreductases. The AOX1 and AOX2 genes are responsible for encoding AOX. Alcohol oxidase is primarily localized in the peroxisome but is also found in the cytoplasm. Alcohol oxidase is a 600 kDa homooctomeric flavoprotein with eight equal 74 kDa subunits; each containing a flavin adenine dinucleotide (FAD) molecule.

Alcohol oxidase has been used:

• to catalyze the oxidation of short-chain, primary, aliphatic alcohols to their respective aldehydes .
• to study methanol metabolism in yeasts, such as Candida, Pichia, and Hansenula.
• to study protein translocation into peroxisomes.
• for the determination of ethanol concentration in alcoholic drinks using enzymatic assay.
• in development of enzyme electrode for the determination of alcohols.

Alcohol oxidase has the highest affinity for methanol. The affinity decreases with increasing chain length of the alkyl (R) group. The enzyme shows little activity toward secondary, tertiary, or aromatic alcohols; or aliphatic alcohols with a chain length of more than 5 carbons. The pH range for activity of this product is 6.5-8.5, with the optimum pH being 7.5. Alcohol oxidases facilitate the conversion of alcohol into carbonyl compounds while producing hydrogen peroxide. It is also the first enzyme in the yeast methanol utilization pathway.

Contains potassium phosphate buffer salts, DTE, and stabilizer

One unit will oxidize 1.0 μmole of methanol to formaldehyde per min at pH 7.5 at 25 °C.