Abstract
We carried out the real-time visualization of individual cellulase molecules using a high-speed atomic force microscopy (HS-AFM), having sub-second time resolution and nanometer space resolution. Trichoderma reesei cellobiohydrolase I (TrCel7A) molecules were observed to slide unidirectionally along the crystalline cellulose surface, and the catalytic domain without the cellulose-binding domain moved with a velocity similar to that of the intact TrCel7A enzyme although inactive mutant did not move, indicating a processive movement of the enzyme driven by the hydrolytic reaction. We also observed traffic jam of enzyme molecules and synergistic degradation of crystalline cellulose using HS-AFM.
