G7907
Galactose Oxidase from Dactylium dendroides
≥30 units/mg solid
Synonym(s):
D-Galactose:oxygen 6-oxidoreductase
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biological source
fungus (Dactylium dendroides)
Quality Level
form
lyophilized
specific activity
≥30 units/mg solid
storage temp.
−20°C
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Related Categories
1 of 4
This Item | G7400 | G7141 | SAE0051 |
|---|---|---|---|
| biological source fungus (Dactylium dendroides) | biological source fungus (Dactylium dendroides) | biological source - | biological source - |
| specific activity ≥30 units/mg solid | specific activity ≥3,000 units/g solid | specific activity 100,000-250,000 units/g solid (without added oxygen) | specific activity ≥35 unit/mg solid |
| form lyophilized | form lyophilized powder | form lyophilized powder | form lyophilized powder |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. −20°C |
| Quality Level 200 | Quality Level 200 | Quality Level 200 | Quality Level 200 |
General description
Application
Galactose Oxidase from Dactylium dendroides has been used as a component for galactose oxidase treatment of arabinogalactan.[5] It has also been used to co-immobilise with peroxidase for the preparation of a biosensor for galactose detection.[1]
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.[6]
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.[2] This free radical enzyme[2] possess high substrate specificity.[1]
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.
Related product
Product No.
Description
Pricing
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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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)
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)
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
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
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