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A6380

Sigma-Aldrich

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:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

biological source

bacterial (Bacillus amyloliquefaciens)

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

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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.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

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

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Vincent T Calabrese et al.
Biotechnology progress, 32(5), 1271-1275 (2016-10-23)
A number of years ago we reported a two-step inactivation mechanism for α-amylase (enzyme) on the basis of theoretical and experimental studies in aqueous solutions. In the first step the metal (Ca2+ ) ion dissociates reversibly from the enzyme followed
Andrzej T Lulko et al.
Applied and environmental microbiology, 73(16), 5354-5362 (2007-06-26)
Transcriptome analysis was used to investigate the global stress response of the gram-positive bacterium Bacillus subtilis caused by overproduction of the well-secreted AmyQ alpha-amylase from Bacillus amyloliquefaciens. Analyses of the control and overproducing strains were carried out at the end
Francesca Gherardi et al.
ACS applied bio materials, 2(11), 5136-5143 (2019-11-18)
Enzyme-based treatments are used in heritage conservation for the effective removal of glues and other damaging organic layers from the surfaces of historic and artistic works. Despite their potential, however, the application of enzymatic treatments is currently limited because of
Sun-Li Chong et al.
Analytical and bioanalytical chemistry, 401(9), 2995-3009 (2011-09-10)
The atmospheric pressure matrix-assisted laser desorption/ionization with ion trap mass spectrometry (AP-MALDI-ITMS) was investigated for its ability to analyse plant-derived oligosaccharides. The AP-MALDI-ITMS was able to detect xylooligosaccharides (XOS) with chain length of up to ten xylopyranosyl residues. Though the
Magdalena Eder et al.
Journal of phycology, 44(5), 1221-1234 (2008-10-01)
The cell wall of the green alga Micrasterias denticulata Bréb. ex Ralfs (Desmidiaceae, Zygnematophyceae, Streptophyta) was investigated to obtain information on the composition of component polysaccharides and proteoglycans to allow comparison with higher plants and to understand cell wall functions

Protocols

Follow our procedure for the determination of alpha-Amylase activity. This enzymatic assay of a-Amylase guides you through the entire process and necessary calculations.

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