This enzyme is from D. Dendroides and is recombinantly produced from Yeast in an animal component free fermentation process.
G7400
Galactose Oxidase from Dactylium dendroides
lyophilized powder, ≥3,000 units/g solid
Synonym(s):
D-Galactose:oxygen 6-oxidoreductase
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biological source
fungus (Dactylium dendroides)
Quality Level
form
lyophilized powder
specific activity
≥3,000 units/g solid
storage temp.
−20°C
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1 of 4
This Item | G7907 | G7141 | G2133 |
|---|---|---|---|
| biological source fungus (Dactylium dendroides) | biological source fungus (Dactylium dendroides) | biological source - | biological source - |
| specific activity ≥3,000 units/g solid | specific activity ≥30 units/mg solid | specific activity 100,000-250,000 units/g solid (without added oxygen) | specific activity ≥100,000 units/g solid (without added oxygen) |
| form lyophilized powder | form lyophilized | 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 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.[3]
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.
The specificity for galactose and other sugars is similar to that described by Avigad.
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.
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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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
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.
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
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Hello, I have bought this enzyme for some assays in our lab in January 2024. I would like to ask how this enzyme is produced? Is it recombinant (E. coli or yeast) or is it directly isolated from Dactilium dendroides? Looking forward to hearing from you!
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