amyloglucosidase

Amyloglucosidase, commonly referred to as glucoamylase, is an extracellular enzyme that catalyzes the hydrolysis of alpha-1,4- and alpha-1,6-glycosidic bonds in starch, dextrins, and related carbohydrates to produce D-glucose. Unlike some amylases that stop at shorter oligosaccharides, amyloglucosidase acts endwise from the non-reducing ends of chains, releasing single glucose units as the final product.

The enzyme is produced by various microorganisms, most notably Aspergillus niger and other fungal species, and is also found in some yeasts. Commercial preparations are widely used in starch processing and the food and beverage industries, where they convert starches into glucose syrups and high-glucose feeds. In brewing and ethanol production, amyloglucosidase helps maximize fermentable sugar yield from starch-rich substrates. It is also employed in baking to adjust dough viscosity and sweetness by increasing glucose content.

Biochemically, amyloglucosidase is a glycoside hydrolase often classified in family GH15. It is typically active under acidic to mildly acidic pH conditions and operates best at moderately elevated temperatures, with properties varying by source and formulation. The enzyme is usually used as a processing aid rather than a direct nutrient, and regulatory agencies assess its safety as a food additive or enzyme preparation.

In summary, amyloglucosidase is a key exo-acting starch-degrading enzyme that releases glucose units from polysaccharides, supporting industrial starch conversion and various fermentation processes. It is commonly marketed as glucoamylase, derived from fungal sources.