Galactose oxidase

Modify Date: 2025-08-25 12:03:11

Galactose oxidase Structure
Galactose oxidase structure
Common Name Galactose oxidase
CAS Number 9028-79-9 Molecular Weight N/A
Density N/A Boiling Point N/A
Molecular Formula N/A Melting Point N/A
MSDS Chinese USA Flash Point N/A

 Use of Galactose oxidase


Galactose oxidase (GOase) from fungus is often used in biochemical studies. Galactose oxidase is a type II copper metalloenzyme, and it containing a single polypeptide. Galactose oxidase catalyzes two-electron oxidation of primary alcohols to their corresponding aldehydes, coupling with the reduction of dioxygen to hydrogen peroxide[1].

 Names

Name Galactose oxidase

 Galactose oxidase Biological Activity

Description Galactose oxidase (GOase) from fungus is often used in biochemical studies. Galactose oxidase is a type II copper metalloenzyme, and it containing a single polypeptide. Galactose oxidase catalyzes two-electron oxidation of primary alcohols to their corresponding aldehydes, coupling with the reduction of dioxygen to hydrogen peroxide[1].
Related Catalog
References

[1]. Carina Figueiredo, et al. Electrochemical studies of galactose oxidase. Electrochemical Science Advances. Volume2, Issue5. October 2022. e2100171.

 Chemical & Physical Properties

Storage condition 20°C

 Safety Information

RIDADR NONH for all modes of transport

 Articles28

More Articles
Functional and anionic cellulose-interacting polymers by selective chemo-enzymatic carboxylation of galactose-containing polysaccharides.

Biomacromolecules 13(8) , 2418-28, (2012)

Carboxylated, anionic polysaccharides were selectively prepared using a combination of enzymatic and chemical reactions. The galactose-containing polysaccharides studied were spruce galactoglucomannan...

Glycoproteomics enabled by tagging sialic acid- or galactose-terminated glycans.

Glycobiology 23(2) , 211-21, (2013)

In this paper, we present two complementary strategies for enrichment of glycoproteins on living cells that combine the desirable attributes of "robust enrichment" afforded by covalent-labeling techni...

In vivo enzyme immobilization by inclusion body display.

Appl. Environ. Microbiol. 76(16) , 5563-9, (2010)

A novel strategy for in vivo immobilization of enzymes on the surfaces of inclusion bodies has been established. It relies on expression in Escherichia coli of the polyhydroxybutyrate synthase PhaC fr...

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