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A6380

Sigma-Aldrich

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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About This Item

Numéro CAS:
9000-90-2
Numéro de classification (Commission des enzymes):
3.2.1.1 (BRENDA, IUBMB)
Numéro CE :
232-565-6
Numéro MDL:
MFCD00081319
Code UNSPSC :
12352204
eCl@ss :
32160410
Nomenclature NACRES :
NA.54

Source biologique

bacterial (Bacillus amyloliquefaciens)

Niveau de qualité

200

Type

Type II-A

Pureté

≥30%

Forme

lyophilized powder

Activité spécifique

≥1,500 units/mg protein (biuret)

Poids mol.

50-55 kDa by SDS-PAGE

Technique(s)

SDS-PAGE: suitable

Solubilité

H2O: soluble 0.1 mg/mL, clear, colorless

Adéquation

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

Application(s)

life science and biopharma

Température de stockage

−20°C

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Catégories apparentées

Description générale

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

Actions biochimiques/physiologiques

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.

Caractéristiques et avantages

  • 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.

Définition de l'unité

1 U setzt 1.0 mg Maltose aus Stärke in 3 Minuten frei bei pH 6.9 und 20 °C.

Notes préparatoires

4× crystallized
Dissolves in water to form a clear, colorless solution at 0.1 mg/mL concentration.

Autres remarques

View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
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.

Substrat

Réf. du produit
Description
Tarif

Pictogrammes

Health hazard
GHS08

Mention d'avertissement

Danger

Mentions de danger

H334

Conseils de prudence

P261 - P284 - P501

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

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

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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
Ajaya K Biswal et al.
Biotechnology for biofuels, 7(1), 11-11 (2014-01-24)
Wood cell walls are rich in cellulose, hemicellulose and lignin. Hence, they are important sources of renewable biomass for producing energy and green chemicals. However, extracting desired constituents from wood efficiently poses significant challenges because these polymers are highly cross-linked
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
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Protocoles

Enzymatic Assay of α-Amylase (EC 3.2.1.1)

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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