A6380

α-Amylase from Bacillus sp.

Type II-A, lyophilized powder, ≥1,500 units/mg protein (biuret)

• Synonym(s): Alpha-Amylase, Glycogenase, 1,4-α-D-Glucan-glucanohydrolase
• CAS Number: 9000-90-2
• EC Number: 3.2.1.1 (BRENDA, IUBMB)
• EC Number: 232-565-6
• MDL number: MFCD00081319
• UNSPSC Code: 12352204
• eCl@ss: 32160410
• NACRES: NA.54

Properties

• biological source: bacterial (Bacillus amyloliquefaciens)
• Quality Level: 200
• type: Type II-A
• Assay: ≥30%
• form: lyophilized powder
• specific activity: ≥1,500 units/mg protein (biuret)
• mol wt: 50-55 kDa by SDS-PAGE
• technique(s): SDS-PAGE: suitable
• solubility: H₂O: soluble 0.1 mg/mL, clear, colorless
• suitability: suitable for hydrolysis, synthesis of oligosaccharides and polysaccharides, and sugar modification
• application(s): life science and biopharma
• storage temp.: −20°C

Description

General description

α-Amylase (1,4-α-d-glucan glucohydrolase), an endo-acting glucanase, is a member of the glycoside hydrolase family 13 (GH13).

α-Amylase, an extracellular enzyme, is present in many animals and plants, and also in microorganisms, such as different Bacillus species.

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.

Unit Definition

One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.

Preparation Note

4× crystallized

Dissolves in water to form a clear, colorless solution at 0.1 mg/mL concentration.

Other Notes

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

Safety Information

• Pictograms: GHS08
• Signal Word: Danger
• Hazard Statements: H334
• Precautionary Statements: P261 - P284 - P501
• Hazard Classifications: Resp. Sens. 1
• Storage Class Code: 11 - Combustible Solids
• WGK: WGK 1
• Flash Point(F): Not applicable
• Flash Point(C): Not applicable
• Personal Protective Equipment: dust mask type N95 (US), Eyeshields, Gloves