G7907
Galactose Oxidase from Dactylium dendroides
≥30 units/mg solid
Synonyme(s) :
D-Galactose:oxygen 6-oxidoreductase
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About This Item
Produits recommandés
Source biologique
fungus (Dactylium dendroides)
Niveau de qualité
Forme
lyophilized
Activité spécifique
≥30 units/mg solid
Température de stockage
−20°C
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Description générale
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.
Actions biochimiques/physiologiques
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.
Définition de l'unité
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.
Forme physique
Lyophilized, contains buffer salts and stabilizer
Notes préparatoires
Chromatographically purified
Inhibiteur
Réf. du produit
Description
Tarif
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
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Groman E V and Gou D
Carbohydrate Research, 301(1-2), 69-76 (1997)
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)
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
Grant E Henderson et al.
Bioconjugate chemistry, 22(5), 903-912 (2011-03-15)
The site-specific modification of proteins is expected to be an important capability for the synthesis of bioconjugates in the future. However, the traditional repertoire of reactions available for the direct modification of proteins suffers from lack of specificity, necessitating costly
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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