Not available outside of the UK & Ireland.

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.

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.

Other Notes

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

Physical form

Suspension in 3.2 M ammonium sulfate solution, pH approximately 6

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.

Unit Definition

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