G7907
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:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-843-7
MDL number:
Specific activity:
≥30 units/mg solid
Biological source:
fungus (Dactylium dendroides)
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.
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.
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Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Listings
Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.
G7907-450UN: + G7907-VAR: + G7907-PH: + G7907-150UN: + G7907-BULK: + G7907-450UN-PW: + G7907-150UN-PW: + G7907PROC:
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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)
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
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
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)
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)
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