β-Glucosidase (BGL)

β-Glucosidase is an enzyme (EC 3.2.1.21) that hydrolyzes β-D-glucosidic bonds in a variety of glycosides, oligosaccharides, and notably cellulose, releasing glucose. It is composed of polypeptide chains with conserved catalytic domains featuring a (β/α)8-barrel fold and critical glutamate residues for nucleophilic and acid/base catalysis at the active site. In nature, these enzymes are crucial for the breakdown of plant biomass, immune defense, symbiosis, and metabolism. In medicine, acid-β-glucosidase (a lysosomal variant known as glucocerebrosidase) is replaced via enzyme therapy to treat Gaucher disease. Industry uses various β-glucosidases for biofuel production, food processing, and cellulose hydrolysis. Their function and specificity depend on their glycoside hydrolase family, substrate preference, and structure, with broad variation among species.

Other names

beta-glucosidaseβ-D-glucoside glucohydrolasecellobiaseBGL

Substrate hydrolysis via a two-step retaining mechanism involving nucleophilic attack and acid/base catalysis by active site glutamate residues. Enzyme replacement drugs restore deficient enzyme activity in lysosomal storage disorders.