Galactose Oxidase from Dactylium dendroides (C15-1291-493)

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.

Galactose oxidase has several applications in bioanalytics and histology. This free radical enzyme possess high substrate specificity.

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.

Physical form

Lyophilized, contains buffer salts and stabilizer

Preparation Note

Chromatographically purified