A novel function for the cellulose binding module of cellobiohydrolase I.

A homogeneous cellulose-binding module (CBM) of cellobiohydrolase I (CBHI) from Trichoderma pseudokoningii S-38 was obtained by the limited proteolysis with papain and a series of chromatographs filtration. Analysis of FT-IR spectra demonstrated that the structural changes result from a weakening and splitting of the hydrogen bond network in cellulose by the action of CBM(CBHI) at 40 degrees C for 24 h. The results of molecular dynamic simulations are consistent with the experimental conclusions, and provide a nanoscopic view of the mechanism that strong and medium H-bonds decreased dramatically when CBM was bound to the cellulose surface. The function of CBM(CBHI) is not only limited to locating intact CBHI in close proximity with cellulose fibrils, but also is involved in the structural disruption at the fibre surface. The present studies provided considerable evidence for the model of the intramolecular synergy between the catalytic domain and their CBMs.