The preparation and production of this product is considered proprietary.
10069
α-Amylase from Bacillus sp.
powder, yellow-brown, ~380 U/mg
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250 MG
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Informacje o tej pozycji
Numer CAS:
UNSPSC Code:
12352204
eCl@ss:
32160410
EC Number:
232-565-6
NACRES:
NA.54
MDL number:
Specific activity:
~380 U/mg
Biological source:
Bacillus sp.
Przejdź do
Pomoc techniczna
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Pozwól nam pomócbiological source
Bacillus sp.
form
powder
specific activity
~380 U/mg
greener alternative product characteristics
Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
sustainability
Greener Alternative Product
color
yellow-brown
greener alternative category
, Enabling
storage temp.
2-8°C
Quality Level
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Ta pozycja | |||
|---|---|---|---|
| biological source Bacillus sp. | biological source - | biological source bacterial (Bacillus amyloliquefaciens) | biological source Bacillus sp. |
| specific activity ~380 U/mg | specific activity ~50 U/mg | specific activity ≥1,500 units/mg protein (biuret) | specific activity ≥400 units/mg protein (Lowry) |
| form powder | form powder | form lyophilized powder | form powder |
| storage temp. 2-8°C | storage temp. 2-8°C | storage temp. −20°C | storage temp. −20°C |
| Quality Level 100 | Quality Level 100 | Quality Level 200 | Quality Level 200 |
| color yellow-brown | color yellow-brown | color - | color - |
General description
α-Amylase (α-1,4-glucan-4-glucanohydrolase) belongs to the glycosyl hydrolase family 13. The two aspartic residues and one glutamic acid residue are the prime catalytic residues of α-amylase.[1] All amylases have three domain regions, namely, domain A with a central (β/α)8 barrel, domain B, and β-structure with a Greek key motif encompassing domain C.[1]
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 hydrolysis research. For more information see the article in biofiles.
Application
α-Amylase from Bacillus sp. has been used:
- as a dispersal enzyme to test degradation of S. aureus biofilms[2],
- in the enzymatic hydrolysis of tapioca starch[3]
- in the enzymolysis of plant-based native and the amorphous granular starches[4]
Heat stability of bacterial α-amylases; Action pattern on sweet potato starch, amylose and amylopectin; Action on native wheat starch.
Biochem/physiol Actions
α-Amylase mediates the hydrolysis of starch, malto-oligosaccharides, and glycogen at the α-D-(1,4)-glucosidic linkages.[1] Bacillus sp. serve as an important cell factory for the heterogeneous production of α-amylase.[5] An extracellular secreted thermostable amylase from the Bacillus subtilis strain has also been reported.[6]
Other Notes
One unit is the amount of enzyme which liberates 1 μmole of maltose per minute at pH 6.9 and 25°C (using Cat. No. 85642 as substrate)
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signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Klasa składowania
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
Cold-water solubility, oil-adsorption and enzymolysis properties of amorphous granular starches
Fang C, et al.
Food Hydrocolloids, 117, 106669-106669 (2021)
Junrong Huang et al.
Carbohydrate polymers, 163, 324-329 (2017-03-08)
After combined hydrolysis by α-amylase and β-amylase at room temperature, spherical blocklets in diameters of 27-60nm were observed on the surface of tapioca starch granules by scanning electron micrography (SEM). Tapioca starch (1%, w/w, db, distilled water) was heated by
P.L. Chang Rupp et al.
Journal of Food Biochemistry, 12, 191-191 (1988)
Masayuki Kagawa et al.
Journal of bacteriology, 185(23), 6981-6984 (2003-11-18)
The crystal structure of Bacillus subtilis alpha-amylase, in complex with the pseudotetrasaccharide inhibitor acarbose, revealed an hexasaccharide in the active site as a result of transglycosylation. After comparison with the known structure of the catalytic-site mutant complexed with the native
Amylase enzyme from Bacillus subtilis S8-18: a potential desizing agent from the marine environment.
Balu Jancy Kalpana et al.
Biotechnology and applied biochemistry, 61(2), 134-144 (2013-05-11)
The present study is aimed at developing an economical medium for the production of α-amylase from Bacillus subtilis S8-18, a marine sediment isolate from Palk Bay, with various agricultural by-products that are cheap and rich in starch. These products include
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What is the production strain of this product?
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In which solution I should to dissolve the alfa amylase? should had ca+2? (for starch degradation)
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This product is soluble in water. No additional calcium is required. For specific applications it may also be prepared in typical sodium or potassium phosphate buffer solutions.
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