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Beta-glucanases are a diverse group of glycoside hydrolase enzymes responsible for the degradation of beta-glucans, which are essential structural polysaccharides in the cell walls of fungi, plants, and certain bacteria. In fungi, these enzymes play critical roles in cell wall remodeling, morphogenesis, and hyphal branching, which are vital for the survival and pathogenicity of organisms like Candida albicans and Aspergillus fumigatus. Due to their absence in the human genome, fungal beta-glucanases, particularly the exo-1,3-beta-glucanase isoform, represent promising therapeutic targets for the development of selective antifungal agents. Conversely, beta-glucanase is also employed as a therapeutic drug or dietary supplement in humans to facilitate the digestion of complex fibers and to disrupt resistant fungal biofilms. In clinical diagnostics, the presence of the enzyme's substrate, (1,3)-beta-D-glucan, serves as a significant biomarker for invasive fungal infections. Beyond medicine, these enzymes are extensively used in the food and beverage industry to reduce the viscosity of grain-based products and enhance nutrient absorption in animal feed. Research into small-molecule inhibitors, such as sesamin, continues to explore their potential in overcoming resistance to current antifungal treatments like azoles and polyenes.
Hydrolysis of internal or terminal beta-1,3-glycosidic bonds in beta-glucan polysaccharides to soften or degrade cell walls.
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