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Merck

A6380

Sigma-Aldrich

α-Amylase from Bacillus sp.

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

Szinonimák:

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

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

CAS-szám:
Enzyme Commission szám:
EC-szám:
MDL-szám:
UNSPSC kód:
12352204
eCl@ss:
32160410
NACRES:
NA.54

biológiai forrás

bacterial (Bacillus amyloliquefaciens)

Minőségi szint

típus

Type II-A

Teszt

≥30%

Forma

lyophilized powder

specifikus aktivitás

≥1,500 units/mg protein (biuret)

molekulatömeg

50-55 kDa by SDS-PAGE

technika/technikák

SDS-PAGE: suitable

oldhatóság

H2O: soluble 0.1 mg/mL, clear, colorless

alkalmasság

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

alkalmazás(ok)

life science and biopharma

tárolási hőmérséklet

−20°C

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Általános leírás

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.

Alkalmazás

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

Biokémiai/fiziológiai hatások

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.

Tulajdonságok és előnyök

  • 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.

Egység definíció

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

Elkészítési megjegyzés

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

Egyéb megjegyzések

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.

szubsztrát

Piktogramok

Health hazard

Figyelmeztetés

Danger

Figyelmeztető mondatok

Óvintézkedésre vonatkozó mondatok

Veszélyességi osztályok

Resp. Sens. 1

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 1

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable

Egyéni védőeszköz

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


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Analitikai tanúsítványok (COA)

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Dokumentumtár megtekintése

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
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
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.

Tudóscsoportunk valamennyi kutatási területen rendelkezik tapasztalattal, beleértve az élettudományt, az anyagtudományt, a kémiai szintézist, a kromatográfiát, az analitikát és még sok más területet.

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