10080
α-Amylase from hog pancreas
powder, ~50 U/mg
Synonyme(s) :
α-Amylase Enzyme
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About This Item
Produits recommandés
Source biologique
hog pancreas
Forme
powder
Activité spécifique
~50 U/mg
Température de stockage
−20°C
Description générale
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
Actions biochimiques/physiologiques
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.
Définition de l'unité
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)
Autres remarques
Optimum pH and temperature 6.9 and 53 °C, respectively; calcium is required for activity and also prevents degradation by trypsin; Characterization.
Mention d'avertissement
Danger
Mentions de danger
Conseils de prudence
Classification des risques
Resp. Sens. 1
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
Certificats d'analyse (COA)
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Les clients ont également consulté
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Journal of food science, 84(8), 2059-2064 (2019-07-25)
The objective of this study was to evaluate the effects of different degree of substitution on structural characteristics and crystalline properties of resistant starch esterfied by L-malic acid. With the deepening of the esterification reaction, malate starches particles became larger
I. Kluh
Collection of Czechoslovak Chemical Communications, 44, 288-288 (1979)
Anna Jakubczyk et al.
BioMed research international, 2014, 438459-438459 (2014-09-25)
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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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