The Carbohydrate Binding Module of TrCel7A Aids in Navigating Hemicellulose Barriers in Plant Cell Walls

binding, suggesting a role for CBM1 in substrate navigation and productive binding site recognition. Kinetic analyses revealed that CBM1 enables a rapid binding mode absent in the truncated variant. Consistent with this, the isolated CBM1 domain had a faster substrate association rate than the isolated catalytic domain. These findings demonstrate that CBM1 enhances cellulase-substrate interactions by accelerating binding and enabling navigation of the complex environment of plant cell walls. Our results emphasize the importance of CBMs in natural cellobiohydrolase function and highlight their value in the design of improved cellulases for industrial biomass conversion.