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Merck

G7907

Galactose Oxidase from Dactylium dendroides

≥30 units/mg solid

Sinónimos:

D-Galactose:oxygen 6-oxidoreductase

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Número CAS:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-843-7
MDL number:
Número CE:
Specific activity:
≥30 units/mg solid
Biological source:
fungus (Dactylium dendroides)
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biological source

fungus (Dactylium dendroides)

form

lyophilized

specific activity

≥30 units/mg solid

storage temp.

−20°C

Quality Level

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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.
The specificity for galactose and other sugars is similar to that described by Avigad.

Physical form

Lyophilized, contains buffer salts and stabilizer

Preparation Note

Chromatographically purified

Other Notes

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

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Clase de almacenamiento

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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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)
Copper metalloenzymes
Comprehensive Natural Products II (2010)
Oliver Spadiut et al.
Microbial cell factories, 9, 68-68 (2010-09-15)
The microbes Escherichia coli and Pichia pastoris are convenient prokaryotic and eukaryotic hosts, respectively, for the recombinant production of proteins at laboratory scales. A comparative study was performed to evaluate a range of constructs and process parameters for the heterologous
Takeshi Ito et al.
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We proposed a low cost fabrication procedure of a poly(methylmethacrylate) (PMMA) column chip. 3D microchannel structure consisting of four columns in a chip for a mother die was fabricated using dry film photoresist and photolithography technique. Electroforming was applied to
Sarah E Deacon et al.
Chembiochem : a European journal of chemical biology, 12(4), 593-601 (2011-01-26)
Galactose oxidase (GO) displays broad primary alcohol substrate specificity and so offers potential for engineering new substrate specificity by directed evolution. Producing variant libraries of sufficient complexity ideally requires expression of functional protein in a host such as Escherichia coli.

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