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Key Documents

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)

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

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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Björn Steinmann et al.
Applied and environmental microbiology, 76(16), 5563-5569 (2010-06-29)
A novel strategy for in vivo immobilization of enzymes on the surfaces of inclusion bodies has been established. It relies on expression in Escherichia coli of the polyhydroxybutyrate synthase PhaC from Cupriavidus necator, which carries at its amino terminus an
Ana Mijovilovich et al.
Physical chemistry chemical physics : PCCP, 13(13), 5600-5604 (2011-02-02)
X-ray Emission Spectroscopy (XES) crossover peaks were shown to be sensitive to the protonation state of solvent molecules in the Zn protein carbonic anhydrase and its model compounds. Here we extend such studies to galactose oxidase models i.e. Cu(ii) open
I H El-Sayed et al.
European review for medical and pharmacological sciences, 15(1), 91-97 (2011-03-09)
Colorectal cancer (CRC) is more common in developed countries and is the third most common cancer among both men and women. CRC provides an attractive model of tumour biology with normal mucosa to adenoma to carcinoma sequence. The TF-antigen (Thomsen-Friedenreich)
Julie B Rannes et al.
Journal of the American Chemical Society, 133(22), 8436-8439 (2011-04-30)
A directed evolution approach has been used for the generation of variants of galactose oxidase (GOase) that can selectively oxidize glycans on glycoproteins. The aldehyde function introduced on the glycans D-mannose (Man) and D-N-acetyl glucosamine (GlcNAc) by the enzyme variants
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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