Alcohol Oxidase from Hansenula sp.

Alcohol Oxidase from Hansenula sp. has been used:

• in the immobilization on amperometric biosensor by glutaraldehyde cross linking
• as a component in pre-mixed hydrogels for the electrode preparation in the biosensors
• in the modification of screen printed Co-phthalocyanine/ Carbon electrode for alcohol biosensor preparation

Alcohol oxidase is used to catalyze the oxidation of short-chain, primary, aliphatic alcohols to their respective aldehydes . It may be used to study methanol metabolism is yeasts, such as Candida, Pichia, and Hansenula. It is useful to study protein translocation into peroxisomes.

Alcohol oxidase has the highest affinity for methanol. The affinity decreases with increasing chain length of the alkyl (R) group. Alcohol oxidase is primarily localized in the peroxisome but is also found in the cytoplasm .

Catalyzes the oxidization of primary alcohols to aldehydes.

Molecular Weight: ~600 kDa
Optimum pH: 8.5
pH Range: 5.5-8.5

K_m values with the following substrates:
Allyl alcohol 33.3 mM
Benzyl alcohol 26.6 mM
Ethanol 16.2 mM
Formaldehyde 2.6 mM
Methanol 2.15 mM
N-Butanol 166 mM
n-Propanol 66 mM

Cofactor: FAD

Inhibitors: 1,4-butynediol (irreversible), propargyl alcohol (irreversible), cyclopropanol, cyclopropanone (suicide substrate), formaldehyde, H₂O₂, hydroxylamine, KBr, KCN, methanol (substrate inhibitor), NaN₃, PCMB, propynal, urea, 4-chloromercuribenzoic acid

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