The kinetic impact of cellulase sub-site specificity on enzymatic cellulose hydrolysis rates has been investigated through the integration of experimentally measured adsorption parameters into a mechanistic kinetic model.  Isothermal titration calorimetry and fluorescence-based binding measurements are used to generate adsorption isotherms that can be used to capture enzyme-substrate interactions within the model.  The influence of the catalytic domain on binding behavior is elucidated, and a sensitivity analysis is used to assess the extent to which adsorption phenomena can be rate-limiting.  Surface heterogeneity is seen to significantly influence the predicted kinetics by altering the efficiency of cellulase-cellulose interactions between raw and pretreated lignocellulosic samples.