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ROAMYGL

Roche

Amyloglucosidase

from Aspergillus niger

Synonym(s):

Glucoamylase, disaccharidase-type-α-D-glucosidase

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About This Item

Enzyme Commission number:
3.2.1.3 (BRENDA, IUBMB)
UNSPSC Code:
12352204

biological source

Aspergillus niger

Quality Level

100

form

suspension

specific activity

~14 units/mg protein (At 25 °C with glycogen as the substrate; standardized with BSA.)

mol wt

Mr 97 kDa

packaging

pkg of 10 mL (10102857001 [100 mg])

manufacturer/tradename

Roche

parameter

55 °C optimum reaction temp.

optimum pH

4.6-4.8

storage temp.

2-8°C

Related Categories

General description

Amyloglucosidase is synthesized by several Aspergillus genus species. It is a disaccharidase–type α-glucosidase. This enzyme is an exo-enzyme and one of the major industrial enzymes. The stability of amyloglucosidase can be increased by immobilization.

Specificity

Cleaves terminal glucoses that are α1,4- or α1,6-linked to an oligo- or polysaccharide of multiple glucose units. The product is D-glucose.
Heat inactivation: Heat inactivation is recommended at 80 °C for 45 minutes, followed by rapidly cooling down.

Application

Amyloglucosidase from Aspergillus niger can be used for the hydrolyzation of terminal α1,4- and α1,6-glucosidic bonds (glucose-glucose bonds) in polysaccharides (e.g., starch, dextrins, glycogen), removing glucose units sequentially from the non-reducing end of the molecule. The enzyme will also cleave maltose and maltosides (maltotriose, maltotetraose, etc.).

Biochem/physiol Actions

Amyloglucosidase from Aspergillus niger is capable of hydrolyzing the α-D-(1-4), the α-D-(1-6), and the α-D-(1-3) glucosidic bonds of oligosaccharides. Amyloglucosidase is an extracellular enzyme that converts starch to dextrins and glucose. The enzyme is used in the starch-processing industry for the commercial production of D-glucose from corn syrups.

Unit Definition

Unit Conversion: One unit (+25 °C; glycogen as substrate) corresponds to 8.6 U (+60 °C; starch as substrate).

Physical form

Suspension in 3.2 M ammonium sulfate solution, pH approximately 6

Other Notes

For life science research only. Not for use in diagnostic procedures.

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 1

flash_point_f

does not flash

flash_point_c

does not flash

Certificates of Analysis (COA)

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A A Amirul et al.
Folia microbiologica, 41(2), 165-174 (1996-01-01)
A. niger produced alpha-glucosidase, alpha-amylase and two forms of glucoamylase when grown in a liquid medium containing raw tapioca starch as the carbon source. The glucoamylases, which formed the dominant components of amylolytic activity manifested by the organism, were purified
Recent Advances in Basic and Applied Aspects of Industrial Catalysis (1998)
High-potency amyloglucosidase-producing mold of the Aspergillus niger group.
Smiley KL, et al.
Applied Microbiology, 12(5), 455-455 (1964)
Recent Advances in Basic and Applied Aspects of Industrial Catalysis (1998)
Guang W Wong et al.
Proceedings of the National Academy of Sciences of the United States of America, 101(28), 10302-10307 (2004-07-03)
Biochemical, genetic, and animal studies in recent years have established a critical role for the adipokine Acrp30/adiponectin in controlling whole-body metabolism, particularly by enhancing insulin sensitivity in muscle and liver, and by increasing fatty acid oxidation in muscle. We describe
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