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G7400

Sigma-Aldrich

Galactose Oxidase from Dactylium dendroides

lyophilized powder, ≥3,000 units/g solid

Synonym(s):

D-Galactose:oxygen 6-oxidoreductase

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

fungus (Dactylium dendroides)

Quality Level

form

lyophilized powder

specific activity

≥3,000 units/g solid

storage temp.

−20°C

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General description

Galactose oxidase is an extracellular copper-containing enzyme, secreted by the deuteromycete fungus Dactylium dendroides. It catalyzes the oxidation of a range of primary alcohols, including D-galactose, to the corresponding aldehyde, with reduction of oxygen to hydrogen peroxide.

Application

Galactose oxidase may be used as an analytical tool for the specific determination of D-galactose in blood plasma, plant extracts, and phospholipids. It could be used for the characterization of terminal D-galactoside units in several polymers.

Biochem/physiol Actions

Galactose oxidase catalyzes the coversion of D-galactose to D-galacto-hexodialdose.
2-Deoxy-D-galactose, lactose, melibiose, raffinose and stachyose react with galactose oxidase in the peroxidase:o-tolidine system.
Essentially no oxidation of D-glucose, L-galactose, L-arabinose or D-glucuronate has been observed.

Unit Definition

One unit will produce a ΔA425 of 1.0 per min at pH 6.0 at 25 °C, in a peroxidase and o-tolidine system. Reaction volume = 3.4 mL. Light path = 1 cm.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Bei Yue et al.
Frontiers in pharmacology, 12, 774560-774560 (2021-11-20)
Irinotecan (CPT11), a broad-spectrum cytotoxic anticancer agent, induces a series of toxic side-effects. The most conspicuous side-effect is gastrointestinal mucositis, including nausea, vomiting, and diarrhea. A growing body of evidence indicates that bacteria β-glucuronidase (GUS), an enzyme expressed by intestinal
Yuling Sun et al.
Biomacromolecules, 22(6), 2595-2603 (2021-05-07)
Antifreeze glycoproteins (AFGPs) are able to bind to ice, halt its growth, and are the most potent inhibitors of ice recrystallization known. The structural basis for AFGP's unique properties remains largely elusive. Here we determined the antifreeze activities of AFGP
Biocatalytic desymmetrization of an atropisomer with both an enantioselective oxidase and ketoreductases.
Bo Yuan et al.
Angewandte Chemie (International ed. in English), 49(39), 7010-7013 (2010-08-18)
Development of a galactose biosensor with galactose oxidase-immobilized epidermis of Solanum lycopersicum: potential point-of-care testing for citrin deficiency in high-prevalence areas.
Hencher H C Lee et al.
Clinica chimica acta; international journal of clinical chemistry, 412(3-4), 391-392 (2010-10-26)
Z Markus et al.
Applied microbiology, 13(5), 686-693 (1965-09-01)
The effects on enzyme production of inoculum size and age, medium composition, and culture conditions were studied in shake flasks and in a pilot-plant fermentor. Using a medium consisting of glucose, yeast extract, and inorganic salts in deionized water, we

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