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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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.
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.
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
Regulatory Information
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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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