MP Biomedicals - 0219015501 - Alcohol Oxidase from Pichea pastoris, 1ku

ITEM #: 13276735
Alcohol o x idase has been detected in several strains of yeast, such as Candida, Pichia, and Hansenula, that utilize methanol as a sole carbon and energy source. Some of these enzymes have been isolated and partially characterized. Alcohol o x idase plays a major role in the metabolism of methanol resulting in the formation of formaldehyde. Primarily localized in the pero x isome, alcohol o x idase has also been found in the cytoplasm. Monomers are synthesized in the cytosol and assembled into octomers in the pero x isome. Octomerization is thought to be chaperone mediated. Alcohol o x idase is of interest for the study of protein translocation into pero x isomes. It catalyzes the o x idation of an alcohol to an aldehyde and hydrogen pero x ide.
Alcohol o x idase is used for qualitative and quantitative determination of methanol or ethanol (blood alcohol) by colorimetric procedures. Unlike present ADH based assays for ethanol in biological specimens, no labile cofactors or trapping agents are required and considerably less enzyme is used per assay. Quantitative determination of alcohol using an o x ygen electrode (enzyme electrode) is also possible. With or without catalase, alcohol o x idase can be used to remove alcohol or scavenge o x ygen. Using dilute methanol, sensitive samples can be sterilized through release of the products formaldehyde and hydrogen pero x ide. The enzyme can also be used to generate H2O2 in radio-iodine labelling procedures.
Alcohol o x idase catalyzes the o x idation of short-chain, primary, aliphatic alcohols to their respective aldehydes. It has the highest affinity for methanol. Alcohol o x idase is involved in the metabolism of methanol, which is important for yeasts that utilize methanol as their sole energy source. Alcohol o x idase is primarily found in the pero x isome but may be present in the cytoplasm as well.
Pkg. Type : Amber Glass Bottle
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