A8220
α-Amylase from Aspergillus oryzae
aqueous solution, ≥800 FAU/g
Synonym(s):
Fungamyl® 800L, 1,4-α-D-Glucan-glucanohydrolase
Sign Into View Organizational & Contract Pricing
All Photos(2)
About This Item
EC Number:
MDL number:
UNSPSC Code:
12352204
eCl@ss:
32160410
NACRES:
NA.54
Recommended Products
biological source
Aspergillus sp. (A. oryzae)
form
aqueous solution
specific activity
≥800 FAU/g
greener alternative product characteristics
Waste Prevention
Design for Energy Efficiency
Learn more about the Principles of Green Chemistry.
sustainability
Greener Alternative Product
greener alternative category
storage temp.
2-8°C
Looking for similar products? Visit Product Comparison Guide
General description
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.
Application
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 Actions
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.
.
.
Other Notes
View more information on enzymes for complex carbohydrate analysis at www.sigma-aldrich.com/enzymeexplorer
Legal Information
A product of Novozyme Corp.
Fungamyl is a registered trademark of Novozymes Corp.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Acute Tox. 4 Oral - Resp. Sens. 1
Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Customers Also Viewed
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.
Towards effective and stable probiotics
Yarullina DR, et al.
The International Journal of Risk & Safety in Medicine, S65-S66 (2015)
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)
Michihiro Sugahara et al.
PloS one, 8(2), e57432-e57432 (2013-03-02)
Currently, there are no versatile and established methods for improving stability of proteins. In an entirely different approach from conventional techniques such as mutagenesis, we attempted to enhance enzyme stability of α-amylase from Aspergillus oryzae using a heavy-atom derivatization technique.
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service