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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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Recent Advances in Basic and Applied Aspects of Industrial Catalysis (1998)
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
High-potency amyloglucosidase-producing mold of the Aspergillus niger group.
Smiley KL, et al.
Applied Microbiology, 12(5), 455-455 (1964)
Nicholson N.
Biodiversity: New Leads for the Pharmaceutical and Agrochemical Industries (2000)
Recent Advances in Basic and Applied Aspects of Industrial Catalysis (1998)
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