A8781
β-Amylase from sweet potato
Sinónimos:
1,4-α-D-Glucan maltohydrolase
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Número CAS:
UNSPSC Code:
41106514
NACRES:
NA.56
EC Number:
232-566-1
MDL number:
Servicio técnico
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powder
Quality Level
mol wt
~200,000
packaging
vial of 15 mg
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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greener alternative category
storage temp.
−20°C
General description
β-Amylase from sweet potato is a tetrameric enzyme with each monomer comprising (α/β) core domain and a C-terminal loop region. It belongs to the glycoside hydrolase family GH14.
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Application
β-Amylase from sweet potato has been used:
- as a molecular weight marker in blue native polyacrylamide gel electrophoresis (PAGE)
- as a standard for calibration curve preparation in size exclusion chromatography
- as a model protein for small-angle X-ray analysis (SAXs)
Biochem/physiol Actions
β-Amylase acts on the polysaccharide α(1,4) glycosidic linkages and releases maltose present in the non-reducing ends. Due to its stability, β-Amylase from sweet potato is used in the immobilized enzyme preparation in combination with agarose beads.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Clase de almacenamiento
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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Contenido relacionado
Instructions
S Teotia et al.
Enzyme and microbial technology, 28(9-10), 792-795 (2001-06-09)
beta-amylases are used in production of maltose syrup. It is shown that sweet potato beta-amylase can be purified by affinity precipitation with alginate with 80% activity yield and 44 fold purification. SDS-PAGE of the purified protein showed a single band
Integration of affinity precipitation with partitioning methods for bioseparation of chitin binding lectins.
Teotia, S. et al.
Food and Bioproducts Processing, 84, 37-43 (2006)
Liyu Tu et al.
Journal of cell science, 119(Pt 24), 5077-5086 (2006-12-13)
The surface of the mammalian urinary bladder is covered by a crystalline, asymmetric unit membrane (AUM) structure that contains the four major uroplakins (UPs): Ia, Ib, II and IIIa. UPIa and UPIb belong to the family of tetraspanins. Although UPIa