Rotation of cellulose ribbons during degradation with fungal cellulase

Degradation of bacterial cellulose with a commercial cellulase, Celluclast 1.5 L (Novo Nordisk), from the fungus Trichoderma reesei, causes a rotational movement of the cellulose microfibrils. Purified cellulases (CBH I, CBH II, and EG II) do not induce rotation of bacterial cellulose, however, ratios of CBH I and EG II do cause rotation of bacterial cellulose. Equimolar amounts of CBH I or CBH II and EG II do not result in motion during degradation. Based on these observations, we provide further evidence supporting, at least on theoretical grounds, the hypothesis that cellulose chains have intrinsic chirality. As the cellulase enzymes interact with and degrade the cellulose fibrils, the crystalline structure of the cellulose is altered, allowing the linear cellulose polymers to relax into a lower energy state, thus relieving the strain induced by crystallization of the nascent beta -glucan chains during the biogenesis of the microfibril. This conversion of crystalline bacterial ribbons into more relaxed conformations produces the rotation observed during the treatment of bacterial cellulose with cellulase.