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A6380

α-Amylase from Bacillus sp.

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

Synonyme(s) :

Alpha-Amylase, Glycogenase, 1,4-α-D-Glucan-glucanohydrolase

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A propos de cet article

Numéro CAS:
UNSPSC Code:
12352204
eCl@ss:
32160410
EC Number:
232-565-6
NACRES:
NA.54
MDL number:
Numéro CE :
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, 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.

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Cet article
10069A10311.03604
assay

≥30%

assay

-

assay

-

assay

-

specific activity

≥1,500 units/mg protein (biuret)

specific activity

~380 U/mg

specific activity

300-1,500 units/mg protein

specific activity

-

biological source

bacterial (Bacillus amyloliquefaciens)

biological source

Bacillus sp.

biological source

-

biological source

-

technique(s)

SDS-PAGE: suitable

technique(s)

-

technique(s)

-

technique(s)

-

suitability

suitable for hydrolysis, synthesis of oligosaccharides and polysaccharides, and sugar modification

suitability

-

suitability

-

suitability

-

form

lyophilized powder

form

powder

form

lyophilized powder

form

solid


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pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Classe de stockage

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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



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Questions

  1. I just wanted to know if this is food grade. I want to use it for developing sorghum milk (starch hydrolysis)

    1 answer
    1. This product is intended for research use only. Currently, a food grade product option is not available.

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