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Literature summary for 3.2.1.26 extracted from
- Untersuchungen zur Thermostabilität immobilisierter Invertase (1986), Acta Biotechnol., 6, 89-99.
No PubMed abstract available
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| sucrose + H2O | - |
Saccharomyces cerevisiae | D-fructose + D-glucose | - |
? |  |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the thermal stability of the enzyme that is covalently bound via glutaraldehyde to a macroporous polystyrene anion-exchanger, silica and porous glass is higher than that of the soluble enzyme. Immobilization of invertase to the polystyrene anion-exchanger by benzoquinone and trichlorotriazine provides enzyme derivatives with lower thermal stability | Saccharomyces cerevisiae |
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