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Literature summary for 1.4.1.20 extracted from
- Supramolecular-mediated immobilization of L-phenylalanine dehydrogenase on cyclodextrin-coated Au electrodes for biosensor applications (2007), Biotechnol. Lett., 30, 26-32.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus badius | - |
- |
- |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the enzyme glycosylated with mono-6-amino-6-deoxy-beta-cyclodextrin and mono-6-(5-carboxypentane-1-carboxamidoyl)-6-deoxy-beta-cyclodextrin contains about 18 mol and 15 mol oligosaccharide per mol of protein and retains 60% and 81% of the initial activity, respectively. The optimum temperature for the catalytic activity is increased in 10°C after attaching the cyclodextrin residues | Bacillus badius |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| additional information | - |
the enzyme glycosylated with mono-6-amino-6-deoxy-beta-cyclodextrin and mono-6-(5-carboxypentane-1-carboxamidoyl)-6-deoxy-beta-cyclodextrin contains about 18 mol and 15 mol oligosaccharide per mol of protein and retains 60% and 81% of the initial activity, respectively. the thermostability profile of the enzyme is improved abd its resistance to thermal inactivation at different temperatures ranging from 45°C to 60°C is noticeably increased after glycosylation | Bacillus badius |
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Release 2023.1 (January 2023)
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