Glükosidaase

Glükosidaase, also written glukosidase in some languages, is a term for enzymes that catalyze the hydrolysis of glycosidic bonds in glycosides, releasing sugar molecules. They belong to the larger family of glycoside hydrolases and are classified within the EC 3.2.1.x series. Glükosidaase enzymes can act on alpha- or beta-glycosidic bonds and may cleave bonds at terminal non-reducing sugar units or within larger polysaccharides, depending on the enzyme and substrate.

In biological systems, glucosidases play diverse roles. In humans, intestinal alpha-glucosidases such as maltases and components of the sucrase-isomaltase complex contribute to carbohydrate digestion by converting disaccharides into monosaccharides like glucose. In lysosomes, beta-glucosidases degrade glucosides and glycosphingolipids; deficiencies of beta-glucosidase activity can lead to storage disorders, including Gaucher disease, caused by glucocerebrosidase deficiency.

Medical and industrial relevance is notable. In medicine, inhibitors of intestinal glucosidases (for example, acarbose and miglitol) slow carbohydrate digestion and help control postprandial blood glucose in type 2 diabetes. In industry, glucosidases are used in biomass conversion, processing of plant-derived glycosides, and flavor development in foods and wines, where they release aromatic aglycones from glycosylated precursors.

Enzymes classified as glucosidases vary in structure and catalytic mechanism. Most utilize acid–base catalysis with active-site residues such as aspartate or glutamate, and they are grouped into several glycoside hydrolase families. Local pH and cellular localization influence their activity.