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A1520

Sigma-Aldrich

α-Amylase Inhibitor from Triticum aestivum (wheat seed)

Type I, lyophilized powder

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About This Item

MDL number:
MFCD00130475
UNSPSC Code:
12352202
NACRES:
NA.77

biological source

Triticum estivum

Quality Level

200

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

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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).

Unit Definition

One unit will reduce the activity of two units of α-amylase (A0521) by 50% after pre-incubation at 25 °C.

Physical form

Lyophilized powder containing buffer salts as sodium phosphate.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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)
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)
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)
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

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