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A7005

Sigma-Aldrich

β-Amylase from sweet potato

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Type I-B, ammonium sulfate suspension, ≥750 units/mg protein (E1%/280)

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

biological source

sweet potato

Quality Level

type

Type I-B

form

ammonium sulfate suspension

specific activity

≥750 units/mg protein (E1%/280)

greener alternative product score

old score: 57
new score: 1
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greener alternative product characteristics

Waste Prevention
Safer Solvents and Auxiliaries
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

sustainability

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concentration

≥7.0 mg/mL

greener alternative category

storage temp.

2-8°C

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General description

β-Amylases belongs to the class of amylolytic enzymes.
We are committed to bringing you Greener Alternative Products, which adhere to one of the four categories of Greener Alternatives . This product belongs to category of Re-engineered products, showing key improvements in Green Chemistry Principles “Waste Prevention”, “Safer Solvents and Auxiliaries” and “Enhanced Energy Efficiency”. Click here to view its DOZN scorecard.
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, from Sigma, has been used in various plant studies, such as carbon starvation studies in Populus tremuloides. β-amylase from sweet potato has been used to examine the utility of the enzyme in inhibiting and removing Staphylococcus aureus biofilms. The enzyme has also been used to prepare β-limit dextrin from waxy maize starch.
β-Amylase from sweet potato has been used:
  • in the hydrolysis of starch and starch-pectin combinations
  • for comparing amylases from different sources in Staphylococcus aureus SH1000 biofilm inhibition and reduction assay
  • for selenium speciation in samples

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. β-amylase from sweet potato is a tetramer of identical subunits, which are arranged to exhibit 222 molecular symmetry.
β-Amylases plays a major role in examining enzymatic promiscuity among glycosidases.

Unit Definition

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

Physical form

Crystalline suspension in 2.3 M (NH4)2SO4

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

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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Effect of cross-linking on the resistance to enzymatic hydrolysis of waxy maize starch and low-methoxy pectin
Khondkar D, et al.
Food Hydrocolloids, 23(2), 387-393 (2009)
Xin Qi et al.
Journal of pharmacy & pharmaceutical sciences : a publication of the Canadian Society for Pharmaceutical Sciences, Societe canadienne des sciences pharmaceutiques, 14(1), 60-66 (2011-04-20)
β-Limit dextrin has been studied for many years as a means to investigate the internal structures of amylose and amylopectin. However its role as an excipient in the pharmaceutical industry has never been reported. This paper is the first one
Mechanisms of enzymatic glycosyl transfer
Comprehensive Natural Products II (2010)
Bradford Craigen et al.
The open microbiology journal, 5, 21-31 (2011-07-16)
Staphylococcus aureus, a versatile human pathogen, is commonly associated with medical device infections. Its capacity to establish and maintain these infections is thought to be related to its ability to form adherent biofilms. In this study, commercially available α-amylase compounds
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

Articles

Instructions for working with enzymes supplied as ammonium sulfate suspensions

Protocols

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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