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A7130

Sigma-Aldrich

β-Amylase from barley

greener alternative

Type II-B, 20-80 units/mg protein (biuret)

Synonym(s):

1,4-α-D-Glucan maltohydrolase

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About This Item

CAS Number:
9000-91-3
Enzyme Commission number:
3.2.1.2 (BRENDA, IUBMB)
EC Number:
232-566-1
MDL number:
MFCD00081391
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type II-B

form

powder

specific activity

20-80 units/mg protein (biuret)

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

shipped in

wet ice

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.

Application

β -Amylase is used to hydrolyze α bonds of α-linked polysaccharides, such as starch and glycogen. β -Amylase, has been used in various plant studies, such as carbon starvation studies in Populus tremuloides . β -Amylase, from barley, has been used to study how pressure and temperature affect catalytic activity .

Biochem/physiol Actions

β-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. Pure, crystalline β-amylase preparation consists of four isoenzymes with different isoelectric points. The enzyme polymerizes very rapidly through the sulfhydryl groups in the absence of reducing agents. p-Chloromercuribenzoate inhibits the polymerization and the enzymatic activity. The reducing agents mercaptoethanol or dithiothreitol can completely restore the activity.

Quality

Crude

Unit Definition

One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 4.8 at 20 °C.

Other Notes

View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Precautionary Statements

P261 - P342 + P311

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

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’.

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Purification and characterisation of crystalline -amylase from barley.
K Visuri et al.
European journal of biochemistry, 28(4), 555-565 (1972-08-04)
Volker Heinz et al.
Biotechnology progress, 21(6), 1632-1638 (2005-12-03)
The depolymerization of starch by beta-amylase during exposure to hydrostatic pressure up to 700 MPa and within a temperature range from 20 to 70 degrees C has been investigated. Inactivation of the enzyme as well as alterations in conversion speed
William R L Anderegg et al.
Plant physiology, 159(4), 1866-1874 (2012-06-06)
Drought impacts on forests, including widespread die-off, are likely to increase with future climate change, although the physiological responses of trees to lethal drought are poorly understood. In particular, in situ examinations of carbon starvation and its interactions with and
Chi-Ho Ngan et al.
Bioinformatics (Oxford, England), 28(2), 286-287 (2011-11-25)
Binding site identification is a classical problem that is important for a range of applications, including the structure-based prediction of function, the elucidation of functional relationships among proteins, protein engineering and drug design. We describe an accurate method of binding
Tomojiro Koide et al.
Bioscience, biotechnology, and biochemistry, 75(4), 793-796 (2011-04-23)
Four putative β-amylase genes found in the Oryza sativa cDNA sequence database (KOME) were expressed in Escherichia coli. Recombinant proteins from two of these genes showed β-amylase activity. Similarly to β-amylases from other plants, the optimum pH of the recombinant
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Protocols

Enzymatic Assay of β-AMYLASE (EC 3.2.1.2)

Beta-amylase is found in bacteria, fungi, and plants. To measure β-amylase activity, this assay uses a colorimetric spectrophotometric stop reaction at 540 nm.

Enzymatic Assay of β-AMYLASE (EC 3.2.1.2)

Beta-amylase is found in bacteria, fungi, and plants. To measure β-amylase activity, this assay uses a colorimetric spectrophotometric stop reaction at 540 nm.

Enzymatic Assay of β-AMYLASE (EC 3.2.1.2)

Beta-amylase is found in bacteria, fungi, and plants. To measure β-amylase activity, this assay uses a colorimetric spectrophotometric stop reaction at 540 nm.

Enzymatic Assay of β-AMYLASE (EC 3.2.1.2)

Beta-amylase is found in bacteria, fungi, and plants. To measure β-amylase activity, this assay uses a colorimetric spectrophotometric stop reaction at 540 nm.

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