A3176
α-Amylase from porcine pancreas
Type VI-B, ≥5 units/mg solid
동의어(들):
alpha-Amylase, β-N-acetylglucosaminidase porcine placenta, PPA, al1,4 glucan-4-glucanohydrolase,, porcine pancreas α-amylase
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크기 선택
제품정보 (DICE 배송 시 비용 별도)
Specific activity:
≥5 units/mg solid
Biological source:
Porcine pancreas
Concentration:
~90% (lactose)
biological source
Porcine pancreas
type
Type VI-B
form
powder
specific activity
≥5 units/mg solid
greener alternative product characteristics
Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
sustainability
Greener Alternative Product
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
storage temp.
2-8°C
Quality Level
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관련 카테고리
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.
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
Analysis Note
Contains lactose
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
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
저장 등급
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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
프로토콜
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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