Glucanases

Glucanases are enzymes that catalyze the hydrolysis of glucans, polysaccharides composed of glucose units linked by glycosidic bonds. They are a broad family of glycoside hydrolases that act on various glucan substrates, including beta-glucans found in fungal and plant cell walls as well as starch-like alpha-glucans. Glucanases can be classified as endo- or exo-acting, and by the type of linkage they cleave, such as beta-1,3-, beta-1,6- or beta-1,4-glucans.

Biological sources and roles: Glucanases are produced by plants, fungi, bacteria, and some yeasts. In plants they are often part of defense responses against pathogens, encoded as pathogenesis-related proteins that degrade fungal cell walls. In fungi and bacteria they participate in cell wall remodeling and nutrient acquisition. In industry, glucanases are employed to modify cell walls, aid fermentation, or convert glucans into soluble sugars.

Applications: In food and beverage production, glucanases improve dough handling and filtration in brewing and wine making by reducing viscosity from beta-glucans. In animal nutrition, they improve feed digestibility by breaking down glucans. In biofuel and textile processing, glucanases help break down plant biomass and processing residues. They are also explored for biocontrol and pharmaceutical uses.

Industrial production: Commercial glucanases are produced by microbial fermentation and available as enzyme preparations with varying pH and temperature optima, stability, and substrate specificity.