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Merck

A8220

Sigma-Aldrich

α-Amylase aus Aspergillus oryzae

greener alternative

aqueous solution, ≥800 FAU/g

Synonym(e):

1,4-α-D-Glucan-glucanohydrolase

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About This Item

EC-Nummer:
EG-Nummer:
MDL-Nummer:
UNSPSC-Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54

Biologische Quelle

Aspergillus sp. (A. oryzae)

Qualitätsniveau

Form

aqueous solution

Spezifische Aktivität

≥800 FAU/g

Grünere Alternativprodukt-Eigenschaften

Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.

sustainability

Greener Alternative Product

Grünere Alternativprodukt-Kategorie

Lagertemp.

2-8°C

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Allgemeine Beschreibung

α-Amylase is also referred as taka-amylase A.
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.

Anwendung

α-Amylase from Aspergillus oryzae has been used:
  • as a positive control in the evaluation of enzyme activity
  • to evaluate its effect on simultaneous saccharification and cofermentation (SSCF) of L-lA by Lactobacillus paracasei LA104{65
  • to study the influence of amylase

  • α-Amylase are suitable various plant studies, such as metabolism studies in Arabidopsis .
  • It is a suitable positive control for the evaluation of exogenous enzymes with amylolytic activity for dairy cows.
  • Amylases from Aspergillus oryzae is a suitable baking additives that prevents staling in the baking industry, clarify haze from fruit juices and alcoholic beverages, and is used to produce glucose and maltose syrup products .

Biochem./physiol. Wirkung

α-Amylase, a digestive enzyme in saliva helps to catalyse the hydrolysis of α-1,4 glycosidic linkages in starch and results in the formation of glucose units. It is effective at slightly alkaline pH and is one of the preferred enzymes for sake brewing.
Aspergillus oryzae α − amylase (Ao α-amylase) enzyme catalyzes the hydrolysis of the α-1,4 glycosidic bonds in soluble starches, and is used in various industrial applications. Natural substrates such as starch and glycogen are broken down into glucose and maltose.
.

Sonstige Hinweise

Rechtliche Hinweise

Ein Produkt der Novozyme Corp.
Fungamyl is a registered trademark of Novozymes Corp.

Piktogramme

Health hazardExclamation mark

Signalwort

Danger

H-Sätze

Gefahreneinstufungen

Acute Tox. 4 Oral - Resp. Sens. 1

Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 3

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

dust mask type N95 (US), Eyeshields, Faceshields, Gloves


Analysenzertifikate (COA)

Suchen Sie nach Analysenzertifikate (COA), indem Sie die Lot-/Chargennummer des Produkts eingeben. Lot- und Chargennummern sind auf dem Produktetikett hinter den Wörtern ‘Lot’ oder ‘Batch’ (Lot oder Charge) zu finden.

Besitzen Sie dieses Produkt bereits?

In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

Molecular biology of the Koji molds
Kitamoto K
Advances in Applied Microbiology, 51, 129-154 (2002)
THE MOUTH, SALIVARY GLANDS AND OESOPHAGUS
Smith ME, et al.
Digestive System, 19-38 (2010)
Towards effective and stable probiotics
Yarullina DR, et al.
The International Journal of Risk & Safety in Medicine, S65-S66 (2015)
I Sander et al.
Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, 37(8), 1229-1238 (2007-07-27)
In order to enable reproducible and comparable exposure measurements of fungal alpha-amylase (alpha-amylase) in different laboratories and countries, the entire procedure from sampling of airborne dust to measuring extracted samples (including standards and the used enzyme) immunoassays must be standardized.
An evaluation of exogenous enzymes with amylolytic activity for dairy cows
Klingerman CM, et al.
Journal of Dairy Science, 92(3), 1050-1059 (2009)

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