10080
α-Amylase from hog pancreas
powder, ~50 U/mg
Synonym(s):
α-Amylase Enzyme
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About This Item
UNSPSC Code:
12352204
EC Number:
232-565-6
NACRES:
NA.54
Specific activity:
~50 U/mg
Biological source:
hog pancreas
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.
Application
α-Amylase from hog pancreas has been used:
- in the in vitro digestion system to study the hydrolysis of pea globulins
- in vitro α-amylase inhibition study
- to prepare digestive juice (salivary juice) for the in vitro model of the human digestion system
Biochem/physiol Actions
α-Amylase is a starch hydrolase, for glucose production, important for energy acquisition. It catalyzes the hydrolysis of α-1,4-glycosidic linkages in starch to form glucose, maltose, and maltotriose units. 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. α-Amylases are widely known industrial enzymes used in food, detergent, textile, fermentation, and pharmaceutical industries.
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.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
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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Limited action of trypsin on porcine pancreatic amylase: characterization of the fragments.
M Granger et al.
FEBS letters, 56(2), 189-193 (1975-08-15)
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I. Kluh
Collection of Czechoslovak Chemical Communications, 44, 288-288 (1979)
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