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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

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About This Item

CAS Number:
9000-90-2
UNSPSC Code:
12352204
eCl@ss:
32160410
EC Number:
232-565-6
NACRES:
NA.54
MDL number:
MFCD00081319
EC Number:
3.2.1.1 (BRENDA, IUBMB)
Specific activity:
≥1,500 units/mg protein (biuret)
Assay:
≥30%
Biological source:
bacterial (Bacillus amyloliquefaciens)
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biological source

bacterial (Bacillus amyloliquefaciens)

Quality Segment

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

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.

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

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Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Codes

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

PPE (personal protective equipment)

dust mask type N95 (US), Eyeshields, Faceshields, Gloves

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

A6380-BULK: + A6380-1G: + A6380-500MG: + A6380-250MG: + A6380-25MG: + A6380-VAR: + A6380-100MG:

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