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Cellulose-binding modules (CBMs) are non-catalytic protein domains found within carbohydrate-active enzymes (CAZymes), such as cellulases and xylanases, that facilitate the association of the enzyme with its insoluble substrate. They are classified into numerous families (e.g., CBM1, CBM2, CBM3) based on amino acid sequence similarity and structural folds, which range from small cystine-knot motifs to larger beta-sandwich structures. While CBMs are primarily known for their role in microbial cellulose degradation by concentrating catalytic domains on the substrate surface, they do not typically serve as direct therapeutic targets for human disease. Instead, they are extensively utilized in biotechnology and medicine as modular tools for protein engineering, purification tags, and targeting moieties in drug delivery systems. In medical research, CBMs have been fused to therapeutic proteins, such as thrombin or cytokines, to create localized delivery systems on cellulose-based scaffolds for applications in wound healing and tissue engineering.
Binding to cellulose surfaces via a planar platform of aromatic residues (typically tyrosine or tryptophan) that facilitate hydrophobic and van der Waals interactions with the pyranose rings of the cellulose polymer.
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