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A6380

Sigma-Aldrich

α-Amylase from Bacillus sp.

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

Sinonimo/i:

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

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About This Item

Numero CAS:
Classificazione EC (Enzyme Commission):
Numero CE:
Numero MDL:
Codice UNSPSC:
12352204
eCl@ss:
32160410
NACRES:
NA.54

Origine biologica

bacterial (Bacillus amyloliquefaciens)

Tipo

Type II-A

Saggio

≥30%

Forma fisica

lyophilized powder

Attività specifica

≥1,500 units/mg protein (biuret)

PM

50-55 kDa by SDS-PAGE

tecniche

SDS-PAGE: suitable

Solubilità

H2O: soluble 0.1 mg/mL, clear, colorless

Compatibilità

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

applicazioni

life science and biopharma

Temperatura di conservazione

−20°C

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Descrizione generale

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.

Applicazioni

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

Azioni biochim/fisiol

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.

Caratteristiche e vantaggi

  • 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.

Definizione di unità

One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.

Nota sulla preparazione

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

Altre note

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.

Substrato

N° Catalogo
Descrizione
Determinazione del prezzo

Pittogrammi

Health hazard

Avvertenze

Danger

Indicazioni di pericolo

Consigli di prudenza

Classi di pericolo

Resp. Sens. 1

Codice della classe di stoccaggio

11 - Combustible Solids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

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


Certificati d'analisi (COA)

Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.

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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
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
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
Applications of high-hydrostatic-pressure processing on microbial enzymes
Liu Y, et al.
Journal of biological and chemical chronicles, 331-371 (2023)

Protocolli

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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