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Merck

A4268

Sigma-Aldrich

α-Amylase from porcine pancreas

greener alternative

Type I-A, PMSF treated, saline suspension, 700-1400 units/mg protein (E1%/280)

Sinónimos:

β-N-acetylglucosaminidase porcine placenta, PPA, al1,4 glucan-4-glucanohydrolase,, porcine pancreas α-amylase

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About This Item

Comisión internacional de enzimas:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

biological source

Porcine pancreas

Quality Level

type

Type I-A

form

saline suspension

specific activity

700-1400 units/mg protein (E1%/280)

mol wt

51-54 kDa

greener alternative product characteristics

Waste Prevention
Design for Energy Efficiency
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sustainability

Greener Alternative Product

technique(s)

activity assay: suitable

suitability

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

application(s)

diagnostic assay manufacturing

greener alternative category

storage temp.

2-8°C

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General description

Molecular mass: 51-54 kDa.
α-Amylase isolated from porcine pancreas is a glycoprotein. It is a single polypeptide chain of ~475 residues containing two SH groups and four disulfide bridges and a tightly bound Ca2+ necessary for stability. Chloride ions are necessary for activity and stability. The pH range for activity is 5.5 to 8.0, with the pH optimum at 7.
We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in starch ethanol research. For more information see the article in biofiles.

Application

α-Amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. α-Amylase, from Sigma, has been used in various plant studies, such as metabolism studies in Arabidopsis .

Biochem/physiol Actions

α-Amylase hydrolyzes the α-(1,4) glucan linkages in polysaccharides of three or more α-(1,4) linked D-glucose units. Natural substrates such as starch and glycogen are broken down into glucose and maltose. α -Amylase, from porcine pancreas, is a glycoprotein that consists of a single polypeptide chain of approximately 475 residues containing 2 SH groups and four disulfide bridges and a tightly bound Ca2+ necessary for stability.

Unit Definition

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

Physical form

Suspension in 2.9 M NaCl solution containing 3 mM CaCl2.

Preparation Note

2× crystallized

inhibitor

Referencia del producto
Descripción
Precios

substrate

Referencia del producto
Descripción
Precios

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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


Certificados de análisis (COA)

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Carbohydrate research, 345(2), 235-242 (2009-12-08)
Amylopectin fine structures were studied following limited hydrolysis of gelatinised waxy maize starch by amylases with a different level of inner chain attack (LICA). This was done by size exclusion chromatography as well as by debranching the (partially hydrolysed) amylopectin
Saber Abdelkader Saidi et al.
Heliyon, 8(12), e11954-e11954 (2022-12-09)
The study evaluated the phytochemical composition of Ephedra alata and its effects on α-amylase and lipase enzymes and diabetic-induced liver-kidney-testes toxicities to determine the anti-diabetic, anti-obesity, and anti-toxic potentials of the plant. Obesity was induced by a high-fat and fructose
Buford L Nichols et al.
The Journal of nutrition, 139(4), 684-690 (2009-02-06)
Starch is the major source of food glucose and its digestion requires small intestinal alpha-glucosidic activities provided by the 2 soluble amylases and 4 enzymes bound to the mucosal surface of enterocytes. Two of these mucosal activities are associated with
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The role of the plant matrix is recognized as the main factor restricting starch digestibility in beans. Several authors have provided insights about the mechanisms behind the reduced starch digestibility in plant matrices. In this study, by means of a

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