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G7907

Sigma-Aldrich

Galactose Oxidase from Dactylium dendroides

≥30 units/mg 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

specific activity

≥30 units/mg solid

storage temp.

−20°C

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General description

Galactose oxidase is a member of radicalcoupled copper oxidases family. It is a fungal secretory enzyme.
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 from Dactylium dendroides has been used as a component for galactose oxidase treatment of arabinogalactan. It has also been used to co-immobilise with peroxidase for the preparation of a biosensor for galactose detection.
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. It may also be useful in the determination of lactose.

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.
Galactose oxidase has several applications in bioanalytics and histology. This free radical enzyme possess high substrate specificity.

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.

Physical form

Lyophilized, contains buffer salts and stabilizer

Preparation Note

Chromatographically purified

inhibitor

Product No.
Description
Pricing

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Development of an immunoassay for larch arabinogalactan and its use in the detection of larch arabinogalactan in rat blood
Groman E V and Gou D
Carbohydrate Research, 301(1-2), 69-76 (1997)
Rapid and sensitive galactose oxidase-peroxidase biosensor for galactose detection with prolonged stability
Tkac J, et al.
BioTechnology: An Indian Journal, 13(12), 931-936 (1999)
A R Shatzman et al.
Journal of bacteriology, 130(1), 455-463 (1977-04-01)
The effects of pH and growth density on the amount of an extracellular enzyme, galactose oxidase, synthesized by the fungus Dactylium dendroides were studied. Growth at a pH below 6.7 caused a decrease in the ability of the organism to
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)
Grant E Henderson et al.
Bioconjugate chemistry, 22(5), 903-912 (2011-03-15)
The site-specific modification of proteins is expected to be an important capability for the synthesis of bioconjugates in the future. However, the traditional repertoire of reactions available for the direct modification of proteins suffers from lack of specificity, necessitating costly

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