| Cat# | DIA-497 |
| Source | Bacilus subtilis |
| Description | Hydrolyzes α-1,4-glycosidic bonds in starch, randomly cleaving amylose and amylopectin into dextrins of various chain lengths and small amounts of low-molecular-weight sugars. This random depolymerization rapidly reduces starch paste viscosity (“liquefaction”), hence the name liquefying enzyme. |
| pH Stability | 4.5-8.0 |
| Optimum pH | 5.2–6.2 |
| Optimum temperature | 60–70 °C |
| Thermal stability | 35–90 °C |
| Stabilizers | Calcium ions enhance the stability of enzymatic activity. In the absence of Ca2+, enzymatic activity is completely lost. |
| Unit Definition | One unit of α-amylase is the amount of enzyme required to release one µmole of p-nitrophenol from blocked p-nitrophenyl-maltoheptaoside per minute (in the presence of excess α-glucosidase) at pH 6.0 and 40 °C. |
| Storage | -20 °C, protected from light |
| Synonyms | Medium-temperature α-amylase |
| Product Overview | Composition: Papain and glucose (containing <1% rennet) |
| Concentration | 4000 U/g |
| Package | 250 g |
| Download Datasheet: |  |
