This product has an optimum pH range of 5–9 and will maintain 98% of activity after 60 minutes at pH 6.2 at 85°C. This material is tested pH 6.9 at boiling temperature for 15 minutes. Please see the link below to review the product datasheet:
https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/297/885/a3403pis.pdf
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Kluczowe dokumenty
A3403
α-Amylase from Bacillus licheniformis
Type XII-A, saline solution, ≥500 units/mg protein (biuret)
Synonim(y):
Termamyl® 2X, 1,4-α-D-Glucan-glucanohydrolase
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500000 UNITS
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4840,00 zł
About This Item
Numer CAS:
Numer MDL:
Kod UNSPSC:
12352204
eCl@ss:
32160410
NACRES:
NA.54
345,00 zł
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Polecane produkty
typ
Type XII-A
Formularz
saline solution
aktywność właściwa
≥500 units/mg protein (biuret)
masa cząsteczkowa
57.6 kDa
charakterystyka ekologicznej alternatywy
Waste Prevention
Design for Energy Efficiency
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sustainability
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kategoria ekologicznej alternatywy
temp. przechowywania
2-8°C
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Opis ogólny
α-Amylase is a member of the endo-amylase family. Its molecular weight is 57.6 kDa. α-Amylase is composed of three functional domains namely A, B and C. Domain A is a barrel-shaped (β/α)8 structure and is the largest domain. Domain B is linked to domain A via disulfide bond and is present between domain A and C. Domain C is composed of β-sheets and is connected to domain A via a polypeptide chain.[1]
We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in starch ethanol research. For more information see the article in biofiles.
We are committed to bringing you Greener Alternative Products, which adhere to one or more of The 12 Principles of Greener Chemistry. This product has been enhanced for energy efficiency and waste prevention when used in starch ethanol research. For more information see the article in biofiles.
Zastosowanie
α-Amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. Product A3403 is from Bacillus licheniformis and is type XII-A. α-Amylase, from Sigma, has been used in various plant studies, such as metabolism studies in Arabidopsis [2].
Działania biochem./fizjol.
α-Amylase hydrolyzes the α-(1,4) glucan linkages in polysaccharides of three or more α-(1,4) linked D-glucose units. Natural substrates such as starch and glycogen are broken down into glucose and maltose.
Przestroga
Reported to be heat stable at temperatures as high as ∼90 °C.
Definicja jednostki
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.
Postać fizyczna
Aqueous solution containing sodium chloride and sucrose
Informacje prawne
A product of Novozyme Corp.
Termamyl is a registered trademark of Novozymes Corp.
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Hasło ostrzegawcze
Danger
Zwroty wskazujące rodzaj zagrożenia
Zwroty wskazujące środki ostrożności
Klasyfikacja zagrożeń
Resp. Sens. 1
Kod klasy składowania
10 - Combustible liquids
Klasa zagrożenia wodnego (WGK)
WGK 2
Temperatura zapłonu (°F)
Not applicable
Temperatura zapłonu (°C)
Not applicable
Środki ochrony indywidualnej
Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter
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Protokoły
Follow our procedure for the determination of alpha-Amylase activity. This enzymatic assay of a-Amylase guides you through the entire process and necessary calculations.
Postępuj zgodnie z naszą procedurą oznaczania aktywności alfa-amylazy. Ten test enzymatyczny a-amylazy prowadzi przez cały proces i niezbędne obliczenia.
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What is the optimal conditions (pH and temperature) for this enzyme to degrade starch? Will it deactivate after heating to 100C?
1 answer-
Helpful?
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Dear Sir or Madam Could you tell me exactly in what solution the a-amylase is provided? Unfortunately only a "saline sucrose solution" is stated. I would need the exact composition in order to prepare a negative control in my assay. kind regards
1 answer-
All that we can disclose is that this product is supplied as an aqueous solution containing sodium chloride and sucrose with >=10 mg/mL protein.
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