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A3176

Sigma-Aldrich

α-Amylase from porcine pancreas

greener alternative

Type VI-B, ≥5 units/mg solid

Synonym(s):

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

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About This Item

Enzyme Commission number:
3.2.1.1 (BRENDA, IUBMB)
EC Number:
232-565-6
MDL number:
MFCD00081319
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

biological source

Porcine pancreas

Quality Level

200

type

Type VI-B

form

powder

specific activity

≥5 units/mg solid

greener alternative product characteristics

Waste Prevention
Design for Energy Efficiency
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sustainability

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concentration

~90% (lactose)

technique(s)

activity assay: suitable

suitability

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

application(s)

life science and biopharma

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 . α-Amylase, from porcine pancreas, has been used to remove starch during the study of starch metabolism and ripening in tomatoes .

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. The pH optimum is at 7.

Packaging

Package size based on α-amylase activity

Quality

Contains lactose

Unit Definition

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

Other Notes

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

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

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

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Certificates of Analysis (COA)

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Massimiliano Carciofi et al.
BMC plant biology, 12, 223-223 (2012-11-23)
Starch is stored in higher plants as granules composed of semi-crystalline amylopectin and amorphous amylose. Starch granules provide energy for the plant during dark periods and for germination of seeds and tubers. Dietary starch is also a highly glycemic carbohydrate
Danish Shahzad et al.
Molecules (Basel, Switzerland), 24(8) (2019-04-20)
A series of symmetrical salicylaldehyde-bishydrazine azo molecules, 5a-5h, have been synthesized, characterized by 1H-NMR and 13C-NMR, and evaluated for their in vitro α-glucosidase and α-amylase inhibitory activities. All the synthesized compounds efficiently inhibited both enzymes. Compound 5g was the most
Xin Huang et al.
Foods (Basel, Switzerland), 9(7) (2020-07-28)
The ingestion of gluten-containing foods can cause wheat-related disorders in up to 15% of wheat consuming populations. Besides the role of gluten, α-amylase/trypsin inhibitors (ATI) have recently been identified as inducers of an innate immune response via toll-like receptor 4
Maria R Romero-Lopez et al.
International journal of molecular sciences, 12(4), 2174-2186 (2011-07-07)
Orange is a tropical fruit used in the juice industry, yielding important quantities of by products. The objective of this work was to obtain a dietary fiber-rich orange bagasse product (DFROBP), evaluate its chemical composition and its use in the
Seyadeh Narges Mazloomi et al.
Foods (Basel, Switzerland), 9(9) (2020-09-06)
In this study, orange seed proteins were hydrolyzed by Alcalase enzyme at different enzyme concentrations 1-3% (v/w) and hydrolysis times (2-5 h), to obtain bioactive peptides showing antioxidant, Angiotensin-converting enzyme (ACE) -inhibitory, and hypoglycemic activities. The highest biological activities (p
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