A3403
α-Amylase from Bacillus licheniformis
Type XII-A, saline solution, ≥500 units/mg protein (biuret)
Synonym(s):
Termamyl® 2X, 1,4-α-D-Glucan-glucanohydrolase
Sign In to View Organizational & Contract Pricing.
Select a Size
About This Item
CAS Number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54
MDL number:
Specific activity:
≥500 units/mg protein (biuret)
type
Type XII-A
form
saline solution
specific activity
≥500 units/mg protein (biuret)
mol wt
57.6 kDa
greener alternative product characteristics
Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
sustainability
Greener Alternative Product
greener alternative category
storage temp.
2-8°C
Quality Level
Looking for similar products? Visit Product Comparison Guide
General description
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.
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.
Application
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 .
Biochem/physiol Actions
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.
Physical form
Aqueous solution containing sodium chloride and sucrose
Other Notes
One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.
Legal Information
A product of Novozyme Corp.
Termamyl is a registered trademark of Novozymes Corp.
Disclaimer
Reported to be heat stable at temperatures as high as ∼90 °C.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
10 - Combustible liquids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Faceshields, Gloves, type ABEK (EN14387) respirator filter
Choose from one of the most recent versions:
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Hisaaki Hiraoka et al.
Animal science journal = Nihon chikusan Gakkaiho, 83(10), 690-695 (2012-10-06)
To improve the performance of the analytical method for neutral detergent fiber in feed with heat-stable α-amylase treatment (aNDFom), the process of adding heat-stable α-amylase, as well as other analytical conditions, were examined. In this new process, the starch in
Zsofia Botyanszki et al.
Biotechnology and bioengineering, 112(10), 2016-2024 (2015-05-08)
Biocatalytic transformations generally rely on purified enzymes or whole cells to perform complex transformations that are used on industrial scale for chemical, drug, and biofuel synthesis, pesticide decontamination, and water purification. However, both of these systems have inherent disadvantages related
Xinyi Huang et al.
Tree physiology, 40(5), 652-666 (2020-02-23)
Globally, soil salinization is becoming increasingly prevalent, due to local hydrogeologic phenomena, climate change and anthropogenic activities. This has significantly curtailed current world food production and limits future production potential. In the prairie region of North America, sulfate salts, rather
Michaelle Chokki et al.
Foods (Basel, Switzerland), 9(4) (2020-04-09)
Momordica charantia Linn. (Cucurbitaceae), the wild variety of bitter melon and Morinda lucida Benth (Rubiaceae) were commonly used as a popular folk medicine in Benin. This research focused to measure the antioxidant and enzyme inhibitory effects of M. charantia and
Bjarte Aarmo Lund et al.
Molecules (Basel, Switzerland), 26(23) (2021-12-11)
The determination of the temperature dependence of enzyme catalysis has traditionally been a labourious undertaking. We have developed a new approach to the classical Arrhenius parameter estimation by fitting the change in velocity under a gradual change in temperature. The
Related Content
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service