10065
αα-Amilase
powder, ~30 U/mg
Sinônimo(s):
1,4-α-D-Glicano glicano-hidrolase
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About This Item
Número CE:
Número MDL:
Código UNSPSC:
12352204
eCl@ss:
32160410
NACRES:
NA.54
Preço e disponibilidade não estão disponíveis no momento.
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Formulário
powder
Nível de qualidade
atividade específica
~30 U/mg
peso molecular
Mr ~51000
temperatura de armazenamento
2-8°C
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Descrição geral
Microbial amylases are exoenzymes and are used in several industrial applications, such as production of bread, maltose syrups, and fermentation of soya sauce, miso etc. α-Amylase isolated from Aspergillus oryzae has been found to have molecular weights of 51kDa (sedimentation and diffusion) and 49kDa (gel filtration).[1]
Aplicação
Ações bioquímicas/fisiológicas
Aspergillus oryzae α-amylase (Ao α-amylase) enzyme catalyzes the hydrolysis of the α-1,4 glycosidic bonds in soluble starches and related subsrates. These substrates are broken down to release short oligosaccharides and α-limit dextrins.[5]
Definição da unidade
1 U corresponds to the amount of enzyme which liberates 1 μmol maltose per minute at pH 6.0 and 25°C (starch acc. to Zulkowsky, Cat. No. 85642, as substrate).
Outras notas
Veja mais informações sobre enzimas para análises de carboidratos complexos em www.sigma-aldrich.com/enzymeexplorer
Palavra indicadora
Danger
Frases de perigo
Declarações de precaução
Classificações de perigo
Acute Tox. 4 Oral - Resp. Sens. 1
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
Equipamento de proteção individual
dust mask type N95 (US), Eyeshields, Faceshields, Gloves
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S Wirsel et al.
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We have cloned three genes (amy1, amy2 and amy3) encoding alpha-amylase in the filamentous fungus Aspergillus oryzae. The established overall sequences have a very high degree of homology, showing divergences mainly in the 3'-untranslated regions. The positions and the sequences
Han Tao et al.
Food chemistry, 190, 588-593 (2015-07-28)
The wheat dough was subjected to freezing/thawing treatment for 0, 3, 7, and 10 cycles and fractionated into non-gluten proteins and starch. High-performance liquid chromatography revealed changes in molecular mass distribution occurred for the extracted non-gluten proteins. As for the
Takagi, T., et al.
The Enzymes, 5, 235- 271 (1971)
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