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Literature summary extracted from
- Stability and catalytic activity of alpha-amylase from barley malt at different pressure-temperature conditions (2007), Biotechnol. Bioeng., 97, 1-11.
General Stability
| EC Number | General Stability | Organism |
|---|---|---|
| 3.2.1.1 | Ca2+ stabilizes under combined pressuretemperature treatments in the range of 0.1800 MPa and 3075°C | Hordeum vulgare |
| 3.2.1.1 | pressure up to 200 MPa significantly stabilizs the enzyme against temperature-induced inactivation | Hordeum vulgare |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.1 | Hordeum vulgare | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.2.1.1 | germinated grain | - |
Hordeum vulgare | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.1 | p-nitrophenyl maltoheptaoside + H2O | a maximum of substrate cleavage was identified at 152 MPa and 64°C, yielding approximately 25% higher substrate conversion after 30 min, as compared to the maximum at ambient pressure and 59°C | Hordeum vulgare | ? | - |
? |  |
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Release 2023.1 (January 2023)
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