betaglycosidases

Betaglycosidases, commonly referred to as beta-glucosidases, are enzymes that hydrolyze beta-glycosidic bonds in beta-D-glucosides, releasing glucose. They are widespread in nature, found in bacteria, fungi, plants, and animals. The best-known role is in cellulose degradation, where beta-glucosidases act on cellobiose and other short beta-glucosides to yield glucose, finishing the breakdown of cellulose in concert with endo- and exo-glucanases. They also act on a broad range of substrates, including aryl beta-glucosides and some glycosylated natural products, thereby releasing aglycones that can affect flavor, odor, or bioactivity.

Beta-glucosidases belong to several glycoside hydrolase families (for example GH1 and GH3), and display diverse properties. They may be secreted into the extracellular space or located in the cytoplasm; some are periplasmic in bacteria. Some enzymes show broad substrate specificity, while others are highly specific for certain beta-glucosides. Many beta-glucosidases operate with retaining or inverting mechanisms, depending on their catalytic machinery.

Industrial and biotechnological relevance is significant: in biofuel production, they convert cellobiose into glucose to allow fermentation; in food and beverage industries, they release aroma aglycones from glycosides to enhance flavor; in medicine, beta-glucosidases can activate glucosidic prodrugs or convert toxins.

Inhibitors include glucose itself and certain mechanism-based inhibitors; understanding regulation and kinetics is important for optimizing processes that rely on these enzymes.