Literature summary for 1.4.1.2 extracted from

Bolivar, J.; Mateo, C.; Rocha-Martin, J.; Cava, F.; Berenguer, J.; Fernandez-Lafuente, R.; Guisan, J.
The adsorption of multimeric enzymes on very lowly activated supports involves more enzyme subunits: Stabilization of a glutamate dehydrogenase from Thermus thermophilus by immobilization on heterofunctional supports (2009), Enzyme Microb. Technol., 44, 139-144.

No PubMed abstract available

Application

Application	Comment	Organism
biotechnology	method describes immobilization of enzymes by the maximum amount of subunits and rigidification of the enzyme subunits involved in the immobilization	Thermus thermophilus

Cloned(Commentary)

Cloned (Comment)	Organism
overexpressed in Escherichia coli	Thermus thermophilus

Organism

Organism	UniProt	Comment	Textmining
Thermus thermophilus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
GDH is readily adsorbed on highly activated anionic exchangers (HAAE), but hardly adsorbed on lowly activated supports (LAAE) or on highly activated epoxy supports. Using amino-epoxy supports, GDH immobilizes on HAAE-epoxy and more slowly on LAAE-epoxy supports. Both immobilized biocatalysts are incubated at pH 10 for different times to increase the multipoint covalent attachment. Lowly activated anionic exchangers-epoxy-GDH is stable at pH 4 and 25°C, the enzyme stability does not depend on the enzyme concentration and does not release any subunit to the supernatant, in opposition to the results obtained using HAAE-epoxy supports	Thermus thermophilus

Purification (Comment)

Organism

GDH is readily adsorbed on highly activated anionic exchangers (HAAE), but hardly adsorbed on lowly activated supports (LAAE) or on highly activated epoxy supports. Using amino-epoxy supports, GDH immobilizes on HAAE-epoxy and more slowly on LAAE-epoxy supports. Both immobilized biocatalysts are incubated at pH 10 for different times to increase the multipoint covalent attachment. Lowly activated anionic exchangers-epoxy-GDH is stable at pH 4 and 25°C, the enzyme stability does not depend on the enzyme concentration and does not release any subunit to the supernatant, in opposition to the results obtained using HAAE-epoxy supports

Thermus thermophilus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-glutamate + H2O + NAD+	-	Thermus thermophilus	2-oxoglutarate + NH3 + NADH	-	?

Subunits

Subunits	Comment	Organism
homotrimer	method not specified	Thermus thermophilus

Synonyms

Synonyms	Comment	Organism
GDH	-	Thermus thermophilus
glutamate dehydrogenase	-	Thermus thermophilus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	lowly activated anionic exchangers-epoxy-GDH is stable at pH 4 and 25°C	Thermus thermophilus
66	-	assay at	Thermus thermophilus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
4	-	lowly activated anionic exchangers-epoxy-GDH is stable at pH 4 and 25°C	Thermus thermophilus
8	-	assay at	Thermus thermophilus

Cofactor

Cofactor	Comment	Organism	Structure
NAD+	-	Thermus thermophilus