AbstractThe possible adsorption sites of cellulases on crystalline cellulose were investigated by molecular graphic representation of a crystal of cellulose and estimation of the accessibility of the various glycosidic bonds to enzymatic attack. The results show that only certain glycosidic bonds of certain surface cellulose chains are susceptible to enzymatic hydrolysis. These preferential sites correlate well with previous electron microscopy observations of the adsorption sites of 1,4-β-D-glucan cellobiohydrolase I (CBHI) from Trichoderma reesei on Valonia cellulose
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