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
• Enzyme Commission 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

View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer

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.

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