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Merck
CN

A4268

Sigma-Aldrich

α-Amylase from porcine pancreas

greener alternative

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

Synonym(s):

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

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About This Item

EC Number:
3.2.1.1 (BRENDA, IUBMB)
MDL number:
MFCD00081319
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

Key Documents

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biological source

Porcine pancreas

Quality Level

300

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

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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

, Enabling

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.

Physical form

Suspension in 2.9 M NaCl solution containing 3 mM CaCl2.

Preparation Note

2× crystallized

Other Notes

One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P342 + P311

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

低风险生物材料
动植物源性产品
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Certificates of Analysis (COA)

Lot/Batch Number
0000420141
0000420141
0000417438
0000417438
0000380972

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Doudou Huang et al.
Drug design, development and therapy, 15, 5001-5010 (2021-12-25)
Diabetes is a common disease caused by a combination of genetic and environmental factors, which was the top three diseases threatening human health. Therefore, it is necessary to seek more efficient hypoglycemic drugs. The main objective of this study was
Lijiao Kan et al.
Food chemistry, 361, 130047-130047 (2021-05-25)
Inhibition of maltase, sucrase, isomaltase and glucoamylase activity by acarbose, epigallocatechin gallate, epicatechin gallate and four polyphenol-rich tea extract from white, green, oolong, black tea, were investigated by using rat intestinal enzymes and human Caco-2 cells. Regarding rat intestinal enzyme
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
Annabel Bijttebier et al.
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
Bjarte Aarmo Lund et al.
Molecules (Basel, Switzerland), 26(23) (2021-12-11)
The determination of the temperature dependence of enzyme catalysis has traditionally been a labourious undertaking. We have developed a new approach to the classical Arrhenius parameter estimation by fitting the change in velocity under a gradual change in temperature. The
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Protocols

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.

α-淀粉酶酶促测定 (EC 3.2.1.1)

可根据此操作规程测定α-淀粉酶的活性。该α-淀粉酶酶促测定将会指导您完成整个过程及必要的计算。

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