A1520
α-Amylase Inhibitor
≥200 inhibitor U/mg protein (using porcine pancreatic α-amylase), ≥1000 inhibitor U/mg protein (using human salivary α-amylase), lyophilized powder
Product Name
α-Amylase Inhibitor from Triticum aestivum (wheat seed), Type I, lyophilized powder
biological source
Triticum estivum
type
Type I
form
lyophilized powder
specific activity
≥1000 inhibitor U/mg protein (using human salivary α-amylase), ≥200 inhibitor U/mg protein (using porcine pancreatic α-amylase)
composition
Protein, 35-65% biuret
storage temp.
−20°C
Quality Level
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General description
α-Amylases are endoglycosidases, that are classified into glycosyl hydrolase family 13 (1-3).
Application
α-Amylase Inhibitor from Triticum aestivum (wheat seed) has been used to determine its effects on salivary gland (SG) amylase activity. It has also been used to inhibit the activity from the extract from Bemisia tabaci.
Biochem/physiol Actions
α-Amylases can hydrolyze α-(1,4)-D-glycosidic linkages. It participates in the breakdown of starch and glycogen. Inhibiting this enzyme can be used as a strategy to treat dental caries, diabetes, obesity and periodontal diseases.
Competitive inhibitor of human salivary α-amylase. KI = 2.9 nM, compared to a KM of 5.9 mM (calculated per mole of α-1,4-linked maltose residues).
Physical form
Lyophilized powder containing buffer salts as sodium phosphate.
Other Notes
One unit will reduce the activity of two units of α-amylase (A0521) by 50% after pre-incubation at 25 °C.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
低风险生物材料
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Demonstration and preliminary characterization of
-amylase in the sweetpotato whitefly, Bemisia
tabaci (Aleyrodidae: Homoptera)
Cohen AC and Hendrix DL
Comparative Biochemistry and Physiology (1994)
Frauke Schocker et al.
International archives of allergy and immunology, 174(1), 17-25 (2017-09-28)
Little is known about breast milk as a vehicle for tolerance development or sensitization to peanuts very early in life. Thus, well-characterized and highly sensitive detection systems for the reliable determination of peanut allergens in breast milk are mandatory. For
alpha-Amylase inhibitors: a review of raw material and isolated compounds from plant source
Sales PM, et al.
J. Pharm. Pharm. Sci., 15(1), 141-183 (2012)
Partial characterization of alpha-amylase in the salivary glands of Lygus hesperus and L. lineolaris
Zeng F and Cohen AC
Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology, 126(1), 9-16 (2000)
A review of alpha-amylase inhibitors on weight loss and glycemic control in pathological state such as obesity and diabetes
Mahmood N
Comparative clinical pathology, 25(6), 1253-1264 (2016)
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