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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:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type II-B

Quality Level

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.

greener alternative category

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.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

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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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)
Xin Li et al.
Journal of industrial microbiology & biotechnology, 38(11), 1837-1843 (2011-04-21)
A moderately halophilic strain LY9 with high amylolytic activity was isolated from soil sample obtained from Yuncheng, China. Biochemical and physiological characterization along with 16S rRNA sequence analysis placed the isolate in the genus Halobacillus. Amylase production started from the
Déborah LeCorre et al.
Biomacromolecules, 13(1), 132-137 (2011-12-03)
Starch nanocrystals (SNCs) are crystalline platelets resulting from the acid hydrolysis of starch. A limiting factor for their more widespread use is their preparation duration. Therefore, this study investigates the possibility of developing an enzymatic pretreatment of starch to reduce
Ambarish Nag et al.
BMC systems biology, 5, 94-94 (2011-06-21)
Higher plants and algae are able to fix atmospheric carbon dioxide through photosynthesis and store this fixed carbon in large quantities as starch, which can be hydrolyzed into sugars serving as feedstock for fermentation to biofuels and precursors. Rational engineering

Protocols

Enzymatic Assay of β-AMYLASE (EC 3.2.1.2)

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