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Literature summary for 1.1.1.1 extracted from
- Covalent immobilization of alcohol dehydrogenase (ADH2) from Haloferax volcanii: how to maximize activity and optimize performance of halophilic enzymes (2014), Mol. Biotechnol., 56, 240-247.
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | immobilization of enzyme on metal-derivatized epoxy Sepabeads. The highest immobilization efficiency (100%) and retention activity (60%) are achieved after 48 h of incubation of the enzyme with Niepoxy Sepabeads support in 100 mM Tris-HCl buffer, pH 8, containing 3 M KCl at 5°C. A significant increase in the stability of the immobilized enzyme is achieved by blocking the unreacted epoxy groups with ethylamine. The immobilization process increases the enzyme stability, thermal activity, and organic solvents. One step purification-immobilization can be carried out on metal chelate-epoxy Sepabeads | Haloferax volcanii |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Haloferax volcanii | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ADH2 | - |
Haloferax volcanii |
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Release 2023.1 (January 2023)
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