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A2910

Sigma-Aldrich

Amyloglucosidase from Aspergillus niger

Isoelectric focusing marker, pI 3.6

Synonym(s):

1,4-α-D-Glucan glucohydrolase, Exo-1,4-α-glucosidase, Glucoamylase

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

Quality Level

form

powder

packaging

vial of 2.0-3.0 mg protein

pI 

3.6

storage temp.

−20°C

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Biochem/physiol Actions

Amyloglucosidase is an exoenzyme which catalyzes the hydrolysis of starch at α-1,4 glycosidic bonds to glucose. It also acts on the α-1,6 linkages and is used along with amylase for effective starch digestion. Use of amyloglucosidase enhances fermentation in bread production. It is widely used in baking, as natural sweetener and in detergent production.

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

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)

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Use of alpha-amylase and amyloglucosidase combinations to minimize the bread quality problems caused by high levels of damaged starch
Barrera G, et al.
Journal of Food Science and Technology, 53(10), 3675-3684 (2016)
Purification and characterization of an amyloglucosidase from an ericoid mycorrhizal fungus (Leohumicola incrustata)
Adeoyo OR, et al.
AMB Express, 8(1), 154-154 (2018)
Amyloglucosidase enzymatic reactivity inside lipid vesicles
Li M, et al.
Journal of Biological Engineering, 1(1), 4-4 (2007)
P M Nunes et al.
American journal of physiology. Endocrinology and metabolism, 303(1), E71-E81 (2012-04-13)
Adipose triglyceride lipase (ATGL) is a lipolytic enzyme that is highly specific for triglyceride hydrolysis. The ATGL-knockout mouse (ATGL(-/-)) accumulates lipid droplets in various tissues, including skeletal muscle, and has poor maximal running velocity and endurance capacity. In this study
Er James et al.
Applied microbiology and biotechnology, 96(2), 385-394 (2012-06-13)
This study demonstrates the potential of Aspergillus niger as a candidate expression system for virus-like particle production using gene fusion. Hepatitis B surface antigen (HBsAg) production, targeted through the secretory pathway in A. niger, resulted in completely assembled and properly

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