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A6941

Sigma-Aldrich

Alcohol Oxidase from Candida boidinii

lyophilized powder, 5-15 units/mg protein

Synonyme(s) :

AOD1, AOX, Alcohol:oxygen oxidoreductase

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About This Item

Numéro CAS:
9073-63-6
Numéro de classification (Commission des enzymes):
1.1.3.13 (BRENDA, IUBMB)
Numéro CE :
232-971-3
Numéro MDL:
MFCD00130452
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.54

Source biologique

fungus (Candida boidinii)

Niveau de qualité

200

Forme

lyophilized powder

Activité spécifique

5-15 units/mg protein

Poids mol.

octomer 600 kDa by sedimentation equilibrium

Solubilité

100 mM potassium phosphate, pH 7.5: soluble 1.0 mg/mL at 25 °C (Cold)

Température de stockage

−20°C

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Description générale

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.

Application

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.

Actions biochimiques/physiologiques

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.

Définition de l'unité

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

Forme physique

Contains potassium phosphate buffer salts, DTE, and stabilizer

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

H R Waterham et al.
The Journal of cell biology, 139(6), 1419-1431 (1998-02-12)
Alcohol oxidase (AOX), the first enzyme in the yeast methanol utilization pathway is a homooctameric peroxisomal matrix protein. In peroxisome biogenesis-defective (pex) mutants of the yeast Pichia pastoris, AOX fails to assemble into active octamers and instead forms inactive cytoplasmic
Erol Akyilmaz et al.
Talanta, 61(2), 113-118 (2008-10-31)
An amperometric biosensor based on catalase enzyme for alcohol determination was developed. To construct the biosensor catalase was immobilized by using gelatin and glutaraldehyde on a Clark type dissolved oxygen (DO) probe covered with a teflon membrane which is sensitive
Alcohol oxidase from Candida boidinii.
H Sahm et al.
Methods in enzymology, 89 Pt D, 424-428 (1982-01-01)
H Gülce et al.
Biosensors & bioelectronics, 17(6-7), 517-521 (2002-04-18)
A new enzyme electrode for the determination of alcohols was developed by immobilizing alcohol oxidase in polvinylferrocenium matrix coated on a Pt electrode surface. The amperometric response due to the electrooxidation of enzymatically generated H(2)O(2) was measured at a constant
Eunji Jang et al.
Biosensors & bioelectronics, 31(1), 529-536 (2011-12-20)
This paper presents a simple method to fabricate a microfluidic biosensor that is able to detect substrates for H(2)O(2)-generating oxidase. The biosensor consists of three components (quantum dot-enzyme conjugates, hydrogel microstructures, and a set of microchannels) that were hierarchically integrated
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Protocoles

Enzymatic Assay of Alcohol Oxidase (EC 1.1.3.13)

To measure alcohol oxidase activity, this assay uses 2,2′-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) and a continuous spectrophotometric rate determination at 405 nm.

Enzymatic Assay of Alcohol Oxidase (EC 1.1.3.13)

To measure alcohol oxidase activity, this assay uses 2,2′-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) and a continuous spectrophotometric rate determination at 405 nm.

Enzymatic Assay of Alcohol Oxidase (EC 1.1.3.13)

To measure alcohol oxidase activity, this assay uses 2,2′-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) and a continuous spectrophotometric rate determination at 405 nm.

Enzymatic Assay of Alcohol Oxidase (EC 1.1.3.13)

To measure alcohol oxidase activity, this assay uses 2,2′-azino-bis-(3-ethylbenzothiazoline-6-sulfonic acid) and a continuous spectrophotometric rate determination at 405 nm.

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