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Literature summary for 1.1.1.2 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.
General Stability
| General Stability | Organism |
|---|---|
| following incubation at 5°C, pH 8.0 (100 mM Tris/HCl buffer), for 24 h with 30% DMSO and 30% methanol the immobilized enzyme retains 55 and 60%, respectively. Upon increasing the incubation time to 72 h the immobilized enzyme retains 55% and 45% activity, respectively | Haloferax volcanii |
| in 3 M KCl the immobilized enzyme retains 80% of its original activity after 9 days at 5°C whereas the free crude enzyme retains 60% under same conditions | Haloferax volcanii |
| the immobilization process (48 h of incubation of the enzyme with Ni-epoxy Sepabeads support in 100 mM Tris-HCl buffer, pH 8, containing 3 M KCl at 5°C) increases the enzyme stability, thermal activity, and organic solvents tolerance when compared to its soluble counterpart, indicating that the immobilization enhances the structural and conformational stability. | Haloferax volcanii |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| KCl | both soluble and immobilized enzymes display an optimum activity at 4 M KCl, and no activity is detected at zero salt concentration | Haloferax volcanii |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Haloferax volcanii | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| one step purification-immobilization on metal chelate-epoxy Sepabeads | Haloferax volcanii |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ethanol + NADP+ | - |
Haloferax volcanii | acetaldehyde + NADPH + H+ | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| HvADH2 | - |
Haloferax volcanii |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
assay at | Haloferax volcanii |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 60 | - |
at 60°C the immobilized enzyme shows 20% higher activity compared to the soluble form | Haloferax volcanii |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 10 | - |
assay at | Haloferax volcanii |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADP+ | - |
Haloferax volcanii | |
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