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Literature summary for 1.4.1.4 extracted from
- Stabilization of the hexameric glutamate dehydrogenase from Escherichia coli by cations and polyethyleneimine (2013), Enzyme Microb. Technol., 52, 211-217 .
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | in presence of polyethyleneimine , the enzyme almost maintains the full initial activity after 2 h under conditions where the untreated enzyme retains only 20% of the initial activity, and the effect of the enzyme concentration on enzyme stability almost disappears. This stabilization is maintained in the pH range 59, but it is lost at high ionic strength. This polyethyleneimine -GDH composite is much more stable than the unmodified enzyme in stirred systems | Escherichia coli |
General Stability
| General Stability | Organism |
|---|---|
| in presence of polyethyleneimine , the enzyme almost maintains the full initial activity after 2 h under conditions where the untreated enzyme retains only 20% of the initial activity, and the effect of the enzyme concentration on enzyme stability almost disappears. This stabilization is maintained in the pH range 59, but it is lost at high ionic strength. | Escherichia coli |
| the stability of this enzyme is increased in the presence of Li+ in concentrations ranging from 1 to 10 mM, 1 M of sodium phosphate, or 1 M ammonium sulfate, and a very significant dependence of the enzyme stability on protein concentration is found | Escherichia coli |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| commercial preparation | - |
Escherichia coli | - |
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