Technical Abstract: Future innovations in applications of industrial enzymes to carbohydrates will require improved knowledge of the mode of action. This chapter explores whether one aspect of enzymatic hydrolysis of saccharides is a twisting distortion of the bonds between adjacent monosaccharides in larger carbohydrate substrates. If such distortion is important, then new enzymes could be engineered that would, for example, increase the distortion for faster reaction. One way to learn if linkage distortion occurs is to survey existing geometries in crystalline carbohydrate-protein complexes. Unusual conformations may be distorted as part of the catalytic action if they are at the active site in an enzyme. A related question is whether twisting of the linkage bonds increases the molecular potential energy. For the present work we have tracked the degree of twisting in hundreds of protein–carbohydrate structures and we have used improved computer modeling studies of cellobiose to obtain energies. The largest apparent distortions were in similar, molecules based on lactose.