A3403

α-Amylase from Bacillus licheniformis

Name: α-Amylase from <I>Bacillus licheniformis</I>
Brand: SIGMA

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

Synonym(s):

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

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About This Item

CAS Number:

9000-85-5

UNSPSC Code:

12352204

eCl@ss:

32160410

NACRES:

NA.54

EC Number:

3.2.1.1 (BRENDA, IUBMB)

MDL number:

MFCD00081319

Product Name

α-Amylase from Bacillus licheniformis, Type XII-A, saline solution, ≥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
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sustainability

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greener alternative category

Enabling,

storage temp.

2-8°C

Quality Level

200

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Proteins & Enzymes

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.

Disclaimer

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

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.

Legal Information

A product of Novozyme Corp.

Termamyl is a registered trademark of Novozymes Corp.

Other Notes

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

pictograms

GHS08

signalword

Danger

hcodes

H334

pcodes

P261 - P284 - P501

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

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Improvement and validation of the method to determine neutral detergent fiber in feed.

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

Engineered catalytic biofilms: Site-specific enzyme immobilization onto E. coli curli nanofibers.

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

Differences in growth and physiological and metabolic responses among Canadian native and hybrid willows (Salix spp.) under salinity stress.

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

Exploring Antioxidant and Enzymes (A-Amylase and B-Glucosidase) Inhibitory Activity of Morinda lucida and Momordica charantia Leaves from Benin.

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

ThermoSlope: A Software for Determining Thermodynamic Parameters from Single Steady-State Experiments.

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

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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.