Skip to Content
Merck
All Photos(3)

Documents

A4551

Sigma-Aldrich

α-Amylase from Bacillus licheniformis

greener alternative

lyophilized powder, 500-1,500 units/mg protein, 93-100% (SDS-PAGE)

Synonym(s):

1,4-α-D-Glucan-glucanohydrolase

Sign Into View Organizational & Contract Pricing
All Photos(3)

About This Item

CAS Number:
9000-85-5
Enzyme Commission number:
3.2.1.1 (BRENDA, IUBMB)
EC Number:
232-560-9
MDL number:
MFCD00081319
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

biological source

Bacillus licheniformis

Quality Level

200

Assay

93-100% (SDS-PAGE)

form

lyophilized powder

specific activity

500-1,500 units/mg protein

mol wt

58-62 kDa

composition

Protein, 60-80% BCA

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

General description

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.

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

Lyophilized powder containing potassium phosphate

substrate

Product No.
Description
Pricing

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

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

Uri Lesmes et al.
Journal of agricultural and food chemistry, 56(13), 5415-5421 (2008-06-12)
This study probed the possible effects of type III resistant starch (RS) crystalline polymorphism on RS fermentability by human gut microbiota and the short chain fatty acids production in vitro. Human fecal pH-controlled batch cultures showed RS induces an ecological
Barman, T.E.
Enzyme Handbook, 2, 560-560 (1969)
Olivier Etienne et al.
Biomacromolecules, 6(2), 726-733 (2005-03-15)
Biomedical devices and modified biomaterial surfaces constitute an expanding research domain in the dental field. However, such oral applications have to face a very particular environment containing specific physiological conditions and specific enzymes. To evaluate their suitability in the development
Nathalie Declerck et al.
Protein engineering, 16(4), 287-293 (2003-05-09)
Bacillus licheniformis alpha-amylase (BLA) is a highly thermostable starch-degrading enzyme that has been extensively studied in both academic and industrial laboratories. For over a decade, we have investigated BLA thermal properties and identified amino acid substitutions that significantly increase or
Imogen Ramsey et al.
Scientific reports, 10(1), 20855-20855 (2020-12-02)
Consumer sensory evaluation, aroma release analysis and biophysical protein analysis were used to investigate the effect of ethanol on the release and perception of flavour in beer (lager and stout) at different ethanol levels (0 and 5% ABV). Consumer study
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.

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