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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

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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

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.

greener alternative category

, Enabling

storage temp.

2-8°C

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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’.

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E G Manzanilla et al.
Journal of animal science, 84(10), 2743-2751 (2006-09-15)
We evaluated the effects of 3 additives, sodium butyrate (AC), avilamycin (AB), and a combination of plant extracts (XT), on the productive performance and the intestinal environment of the early-weaned pig. The XT was a standardized mixture with 5% (wt/wt)
Nathalie Wuyts et al.
Plant methods, 6, 17-17 (2010-07-06)
Despite the wide spread application of confocal and multiphoton laser scanning microscopy in plant biology, leaf phenotype assessment still relies on two-dimensional imaging with a limited appreciation of the cells' structural context and an inherent inaccuracy of cell measurements. Here
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
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
Benjamin D Hesse et al.
Tree physiology, 39(2), 192-200 (2018-11-06)
Phloem sustains maintenance and growth processes through transport of sugars from source to sink organs. Under low water availability, tree functioning is impaired, i.e., growth/photosynthesis decline and phloem transport may be hindered. In a 3-year throughfall exclusion (TE) experiment on
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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.

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