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10080

α-Amylase from hog pancreas

powder, ~50 U/mg

Sinónimos:

α-Amylase Enzyme

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Tamaño de envaseSKUDisponibilidadPrecio
25 g
Comprobar disponibilidad del carrito
US$ 95,10
100 g
Comprobar disponibilidad del carrito
US$ 288,00

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UNSPSC Code:
12352204
EC Number:
232-565-6
NACRES:
NA.54
Specific activity:
~50 U/mg
Biological source:
hog pancreas

US$ 95,10

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biological source

hog pancreas

Quality Level

form

powder

specific activity

~50 U/mg

storage temp.

−20°C

General description

Pancreatic α-amylase is produced by the pancreatic acinar cells and released into the duodenum. It is a major molecule of pancreatic fluid.[1]

Application

α-Amylase from hog pancreas has been used:
  • in the in vitro digestion system to study the hydrolysis of pea globulins[2]
  • in vitro α-amylase inhibition study[3]
  • to prepare digestive juice (salivary juice) for the in vitro model of the human digestion system[4]

Biochem/physiol Actions

α-Amylase is a starch hydrolase, for glucose production, important for energy acquisition.[5] It catalyzes the hydrolysis of α-1,4-glycosidic linkages in starch to form glucose, maltose, and maltotriose units.[1] In mammals, α-amylase regulates the sugar assimilation by reducing the glucose uptake by Na+/glucose cotransporter 1 (SGLT1) and stimulating glycoprotein N-glycans mediated starch digestion. α-Amylase inhibitors are associated with the treatment of type 2 diabetes mellitus.[1] α-Amylases are widely known industrial enzymes used in food, detergent, textile, fermentation, and pharmaceutical industries.[1]

Other Notes

1 U corresponds to the amount of enzyme which liberates 1 μmol maltose per minute at pH 6.9 and 25°C (starch acc. to Zulkowsky, Cat. No. 85642, as substrate)
Optimum pH and temperature 6.9 and 53 °C, respectively; calcium is required for activity and also prevents degradation by trypsin; Characterization.

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Este artículo
A317610069A6380
biological source

hog pancreas

biological source

Porcine pancreas

biological source

Bacillus sp.

biological source

bacterial (Bacillus amyloliquefaciens)

specific activity

~50 U/mg

specific activity

≥5 units/mg solid

specific activity

~380 U/mg

specific activity

≥1,500 units/mg protein (biuret)

form

powder

form

powder

form

powder

form

lyophilized powder

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

−20°C

Quality Level

100

Quality Level

200

Quality Level

100

Quality Level

200


pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Clase de almacenamiento

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



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Muhammad H Alu'datt et al.
Food chemistry, 240, 784-798 (2017-09-28)
This investigation was performed to assess the effects of sonication on the structure of protein, extractability of phenolics, and biological properties of isolated proteins and protein co-precipitates prepared from brewers' spent grain and soybean flour. Scanning electron micrographs revealed that
Paula Monteiro de Souza et al.
Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology], 41(4), 850-861 (2010-10-01)
Amylases are one of the main enzymes used in industry. Such enzymes hydrolyze the starch molecules into polymers composed of glucose units. Amylases have potential application in a wide number of industrial processes such as food, fermentation and pharmaceutical industries.
Kimie Date et al.
The Journal of biological chemistry, 290(28), 17439-17450 (2015-05-30)
α-Amylase, a major pancreatic protein and starch hydrolase, is essential for energy acquisition. Mammalian pancreatic α-amylase binds specifically to glycoprotein N-glycans in the brush-border membrane to activate starch digestion, whereas it significantly inhibits glucose uptake by Na(+)/glucose cotransporter 1 (SGLT1)



Número de artículo de comercio global

SKUGTIN
10080-25G04061838664273
10080-100G04061838664266

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