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:
Specific activity:
≥1,500 units/mg protein (biuret)
Assay:
≥30%
Biological source:
bacterial (Bacillus amyloliquefaciens)
Service technique
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bacterial (Bacillus amyloliquefaciens)
Quality Level
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.
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
signalword
Danger
hcodes
pcodes
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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Contenu apparenté
Instructions
Immobilized Enzymes on Gold Nanoparticles: From Enhanced Stability to Cleaning of Heritage Textiles.
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
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
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