Carbohydrate-binding modules recognizing β-glucan (CBM)

Carbohydrate-binding modules (CBMs) that recognize β-glucan are non-catalytic protein domains typically found within multi-modular carbohydrate-active enzymes (CAZymes), such as glucanases and cellulases. These modules function by specifically binding to various β-glucan structures, including β-1,3-glucans (e.g., laminarin, curdlan), β-1,4-glucans (e.g., cellulose), and mixed-linkage β-1,3-1,4-glucans. Their primary biological role is to tether the parent enzyme to its polysaccharide substrate, increasing the local concentration of the enzyme and thereby enhancing the efficiency of the catalytic domain through a proximity effect. While CBMs are predominantly found in bacteria, fungi, and plants, they are of significant interest in biotechnology for biomass conversion and as molecular probes for detecting specific glycans in complex biological samples. In a medical context, they are not traditional human therapeutic targets but are explored as tools for targeted drug delivery to fungal cell walls or as components of diagnostic assays for fungal infections. They should be distinguished from human β-glucan receptors like Dectin-1, which initiate immune signaling upon binding.

Other names

Beta-glucan binding modulesGlucan-binding domainsCBM families (4, 6, 11, 13, 32, 39, 43, 44, 46, 52, 54, 56, 65, 72, 76, 79, 80, 81, 85)Carbohydrate-binding module

Substrate binding and enzyme targeting