Skip to Content
Merck
All Photos(2)

Key Documents

View All Documentation

A3403

Sigma-Aldrich

α-Amylase from Bacillus licheniformis

greener alternative

Type XII-A, saline solution, ≥500 units/mg protein (biuret)

Synonym(s):

Termamyl® 2X, 1,4-α-D-Glucan-glucanohydrolase

Sign Into View Organizational & Contract Pricing
All Photos(2)

About This Item

CAS Number:
9000-85-5
Enzyme Commission number:
3.2.1.1 (BRENDA, IUBMB)
MDL number:
MFCD00081319
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

type

Type XII-A

Quality Level

200

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

Enabling,

storage temp.

2-8°C

Looking for similar products? Visit Product Comparison Guide

Related Categories

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.

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.

Caution

Reported to be heat stable at temperatures as high as ∼90 °C.

Unit Definition

One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 6.9 at 20 °C.

Physical form

Aqueous solution containing sodium chloride and sucrose

Legal Information

A product of Novozyme Corp.
Termamyl is a registered trademark of Novozymes Corp.

substrate

Product No.
Description
Pricing

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P284 - P501

Hazard Classifications

Resp. Sens. 1

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

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’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit 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
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
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
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
Laura Escrivá et al.
Toxins, 14(1) (2022-01-21)
The presence of mycotoxins in cereals and cereal products remains a significant issue. The use of natural ingredients such as pumpkin and whey, which contain bioactive compounds, could be a strategy to reduce the use of conventional chemical preservatives. The
View All Related Papers

Protocols

Enzymatic Assay of α-Amylase (EC 3.2.1.1)

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.

Enzymatic Assay of α-Amylase (EC 3.2.1.1)

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.

Enzymatic Assay of α-Amylase (EC 3.2.1.1)

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.

Enzymatic Assay of α-Amylase (EC 3.2.1.1)

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.

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