A7005
β-Amylase from sweet potato
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
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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
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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
Other Notes
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
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)
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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
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
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)
Mechanisms of enzymatic glycosyl transfer
Comprehensive Natural Products II (2010)
C G Cheong et al.
Proteins, 21(2), 105-117 (1995-02-01)
Sweet potato beta-amylase is a tetramer of identical subunits, which are arranged to exhibit 222 molecular symmetry. Its subunit consists of 498 amino acid residues (Mr 55,880). It has been crystallized at room temperature using polyethylene glycol 1500 as precipitant.
Articles
Instructions for working with enzymes supplied as ammonium sulfate suspensions
Protocols
Enzymatic Assay of β-AMYLASE (EC 3.2.1.2)
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