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A7130

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
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-566-1
MDL number:
MFCD00081391
EC Number:
3.2.1.2 (BRENDA, IUBMB)

Key Documents

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Product Name

β-Amylase from barley, Type II-B, 20-80 units/mg protein (biuret)

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

Quality Level

200

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1 of 4

This Item
A985710070A4551
β-Amylase from barley Type II-B, 20-80 units/mg protein (biuret)

Sigma-Aldrich

A7130

β-Amylase from barley

α-Amylase from Aspergillus oryzae ≥150 units/mg protein (biuret)

Sigma-Aldrich

A9857

α-Amylase from Aspergillus oryzae

α-Amylase from Bacillus sp. powder, yellow-brown, ~50 U/mg

Sigma-Aldrich

10070

α-Amylase from Bacillus sp.

α-Amylase from Bacillus licheniformis lyophilized powder, 500-1,500 units/mg protein, 93-100% (SDS-PAGE)

Sigma-Aldrich

A4551

α-Amylase from Bacillus licheniformis

specific activity

20-80 units/mg protein (biuret)

specific activity

≥150 units/mg protein (biuret)

specific activity

~50 U/mg

specific activity

500-1,500 units/mg protein

form

powder

form

powder

form

powder

form

lyophilized powder

shipped in

wet ice

shipped in

-

shipped in

-

shipped in

-

storage temp.

2-8°C

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

Quality Level

200

Quality Level

200

Quality Level

100

Quality Level

200

type

Type II-B

type

-

type

-

type

-

Analysis Note

Crude

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 [1]. β -Amylase, from barley, has been used to study how pressure and temperature affect catalytic activity [2].

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.[3]

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.

Other Notes

One unit will liberate 1.0 mg of maltose from starch in 3 min at pH 4.8 at 20 °C.
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer

pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves

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Certificates of Analysis (COA)

Lot/Batch Number
0000492669
0000492669
0000448370
0000448371
0000448369

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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
Purification and characterisation of crystalline -amylase from barley.
K Visuri et al.
European journal of biochemistry, 28(4), 555-565 (1972-08-04)
Jun Li et al.
Molecular plant-microbe interactions : MPMI, 24(10), 1165-1178 (2011-06-09)
Microbial volatiles promote the accumulation of exceptionally high levels of starch in leaves. Time-course analyses of starch accumulation in Arabidopsis leaves exposed to fungal volatiles (FV) emitted by Alternaria alternata revealed that a microbial volatile-induced starch accumulation process (MIVOISAP) is
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
Heike Reinhold et al.
The Plant cell, 23(4), 1391-1403 (2011-04-14)
Plants contain β-amylase-like proteins (BAMs; enzymes usually associated with starch breakdown) present in the nucleus rather than targeted to the chloroplast. They possess BRASSINAZOLE RESISTANT1 (BZR1)-type DNA binding domains--also found in transcription factors mediating brassinosteroid (BR) responses. The two Arabidopsis
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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.

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