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Merck

A7005

β-アミラーゼ from sweet potato

greener alternative

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

別名:

1,4-α-D-グルカン マルトヒドロラーゼ

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この商品について

CAS番号:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-566-1
MDL number:
EC Number:
Specific activity:
≥750 units/mg protein (E1%/280)
Biological source:
sweet potato
Concentration:
≥7.0 mg/mL
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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
Find out more about DOZN™ Scoring

greener alternative product characteristics

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

sustainability

Greener Alternative Product

concentration

≥7.0 mg/mL

greener alternative category

storage temp.

2-8°C

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 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

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.

Biochem/physiol Actions

β-Amylases plays a major role in examining enzymatic promiscuity among glycosidases.
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.

Physical form

2.3 Mの(NH4)2SO4溶液で調製した結晶性懸濁液

Other Notes

1ユニットは、pH 4.8、20°C、3分間に、1.0 mgのマルトースをデンプンから遊離させる酵素量です。
より詳細な情報につきましては、www.sigma-aldrich.com/enzymeexplorerenzymes for complex carbohydrate analysisをご覧ください。


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pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

保管分類

11 - Combustible Solids

wgk

WGK 3



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プロトコル

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.

資料

硫酸アンモニウム懸濁液として提供される酵素の使用方法

Instructions for working with enzymes supplied as ammonium sulfate suspensions


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)