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
Sign In to View Organizational & Contract Pricing.
Select a Size
Change View
About This Item
CAS Number:
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)
biological source
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
Still not finding the right product?
Explore all of our products under α-Amylase from Bacillus sp.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
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
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Related Content
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
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
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