Amyloglukosidas

Amyloglukosidas, more commonly known as glucoamylase, is an enzyme that catalyzes the hydrolysis of starch-derived alpha-1,4- and alpha-1,6-glycosidic linkages to produce glucose. It is an exo-enzyme that removes glucose units from the non-reducing ends of starch chains, complementing other amylolytic enzymes such as alpha-amylase. In many contexts, glucoamylase and amyloglucosidase refer to the same enzyme (EC 3.2.1.3).

Natural occurrence and sources include fungi, yeast, and certain bacteria that secrete the enzyme for extracellular digestion of starch. Industrially important producers include Aspergillus niger, Aspergillus awamori, and Rhizopus species, which generate large quantities of thermostable, commercially usable preparations. In animals and humans, a brush-border enzyme called glucoamylase participates in dietary starch digestion, illustrating a physiological role for this activity beyond industrial applications.

Biochemical properties vary with source, but glucoamylases generally function best in acidic to near-neutral pH ranges and can be thermostable depending on their origin and processing. The enzyme is used industrially to saccharify starch, converting it to glucose syrups and high-fructose syrups as part of starch processing, brewing, and food production. It is often applied in combination with other amylolytic enzymes to maximize glucose yield from starch.

See also: amylase, maltase, carbohydrate digestion, starch hydrolysis.