Merck, A6380-1G, α-Amylase from Bacillus sp.

General description
α-Amylase, an extracellular enzyme, is present in many animals and plants, and also in microorganisms, such as different Bacillus species.
α-Amylase (1,4-α-d-glucan glucohydrolase), an endo-acting glucanase, is a member of the glycoside hydrolase family 13 (GH13).
Application
α-Amylase from Bacillus sp. has been used:

as a component of salivary fluid to perform artificial mastication; in luminal gastrointestinal digestion experiment
as a standard in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to determine the concentration of α-Amylase
to de-starch the alcohol insoluble residue (AIR) for non-cellulosic neutral monosaccharide analysis

Biochem/physiol Actions
α-Amylase degrades starch into oligosaccharides such as maltose, and glucose and alpha limit dextrin. It hydrolyzes the α-(1→4) glucosidic linkages in polysaccharides of three or more α-(1→4) linked D-glucose units, without hydrolyzing the α-(1→6) bond. It participates in glucose production and is essential for energy acquisition. α-Amylases are widely known industrial enzymes used in the food, detergent, textile, fermentation, and pharmaceutical industries.
Features and Benefits
α-Amylase from Bacillus licheniformis NCIB 6346 retains over 98% of its activity after 60 minutes at pH 6.2 and 85°C.
Other α-Amylase maintain 100% of their activity after storage for 1 hour at 91°C.

Maintains >98% of activity after 60 minutes at pH 6.2 at 85 °C.
Preparation Note
4× crystallized
Dissolves in water to form a clear, colorless solution at 0.1 mg/mL concentration.
Other Notes
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.
This product is for R&D use only, not for drug, household, or other uses. Please consult the Safety Data Sheet for information regarding hazards and safe handling practices.
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer