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Amyloglucosidase from Aspergillus niger

greener alternative

powder, white, ~120 U/mg

Glucoamylase, 1,4-α-D-Glucan glucohydrolase, Exo-1,4-α-glucosidase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:



specific activity

~120 U/mg

mol wt

Mr ~97000

greener alternative product characteristics

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



foreign activity

protease ≤0.1%

greener alternative category


storage temp.


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General description

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.

Unit Definition

1 U corresponds to the amount of enzyme which liberates 1 μmol glucose per minute at pH 4.8 and 60 °C (starch, Cat. No. 85642, as substrate).

Other Notes

Synthesis of hetero-oligosaccharides by glucoamylase in reverse.


Health hazard

Signal Word


Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificate of Analysis

Enter Lot Number to search for Certificate of Analysis (COA).

Certificate of Origin

Enter Lot Number to search for Certificate of Origin (COO).

More documents

Quotes and Ordering

  1. Which document(s) contains shelf-life or expiration date information for a given product?

    If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

  2. How do I get lot-specific information or a Certificate of Analysis?

    The lot specific COA document can be found by entering the lot number above under the "Documents" section.

  3. How do I find price and availability?

    There are several ways to find pricing and availability for our products. Once you log onto our website, you will find the price and availability displayed on the product detail page. You can contact any of our Customer Sales and Service offices to receive a quote.  USA customers:  1-800-325-3010 or view local office numbers.

  4. What is the Department of Transportation shipping information for this product?

    Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product. 

  5. What is the molecular weight of Product 10113, Amyloglucosidase from Aspergillus niger?

    Amyloglucosidase from A. niger exists in two isoforms with MWs of 69,810 and 89,130, as determined by SDS-PAGE. See: Starch, 34, 346 (1982).

  6. Does Product 10113,  Amyloglucosidase from Aspergillus niger, contain any stabilizers or additives?

    No extending additives such as glucose or sucrose are added. It is unknown if the starting material contained any additives. This product does not contain sodium acetate buffer salts.

  7. How can a solution of Product 10113,  Amyloglucosidase from Aspergillus niger, be prepared?

    A 1 mg/mL solution may be prepared in 10 mM sodium acetate buffer at approximately pH 4.8.

  8. My question is not addressed here, how can I contact Technical Service for assistance?

    Ask a Scientist here.

R.A. Rastall et al.
Biotechnology Letters, 13, 501-501 (1991)
Tiziana Ventriglia et al.
Plant physiology, 148(1), 65-76 (2008-07-11)
ADP-glucose (Glc) pyrophosphorylase (ADP-Glc PPase) catalyzes the first committed step in starch biosynthesis. Higher plant ADP-Glc PPase is a heterotetramer (alpha(2)beta(2)) consisting of two small and two large subunits. There is increasing evidence that suggests that catalytic and regulatory properties
Thomas Hundsberger et al.
Journal of neurology, 260(9), 2279-2285 (2013-06-12)
Glycogen storage disease type II is a rare multi-systemic disorder characterised by an intracellular accumulation of glycogen due a mutation in the acid alpha glucosidase (GAA) gene. The level of residual enzyme activity, the genotype and other yet unknown factors
Juan Antonio Tamayo-Ramos et al.
Biotechnology and bioengineering, 110(2), 543-551 (2012-09-06)
In filamentous fungi, most of the strategies used for the improvement of protein yields have been based on an increase in the transcript levels of a target gene. Strategies focusing at the translational level have been also described, but are
Ting-Ying Jiang et al.
PloS one, 7(7), e41131-e41131 (2012-07-21)
The N-terminal starch binding domain of Rhizopus oryzae glucoamylase (RoSBD) has a high binding affinity for raw starch. RoSBD has two ligand-binding sites, each containing a ligand-binding clamp: a polyN clamp residing near binding site I is unique in that

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