Abstract: The cellulase adsorbed and formed enzyme-substrate(ES) compound is a key step in the process of enzymatic hydrolysis.Through the comparison of cellulase adsorbed on two substrates: microcrystalline cellulose(MCC) with high degree of crystallinity and decrystallization microcrystalline cellulose(D-MCC) with low degree of crystallinity, it was found that, in the XPS wide scan patterns of adsorption equilibrium MCC, a new absorption peak of nitrogen element(399.06 eV) was observed.The fitting method is adopted to treat the strong peak of XPS-O1s, and the binding energy of this new peak was only 530.53 eV.In the infrared absorption range of 3050-3550 cm-1, the absorption intensity of OH group decreased with extending adsorption time on cellulose.The above results proved that new hydrogen bonds (C-OH…NH) between the protein amino(-NH2) and cellulose molecule chain(-OH) were generated during the cellulose adsorption process.From the comparison of the adsorption rate curves between MCC and D-MCC, the decrystallization method to improve cellulase adsorption was more effective than enhancing the temperature.From the comparison of adsorption kinetics between MCC and D-MCC at 35℃, it was indicated that a reduction of cellulose crystallinity was positive for adsorption rate.MCC with rigid surface was fit for the first-order kinetic hypothesis.D-MCC with flexible surface was not suitable for the first-order kinetic.A more suitable kinetic hypothesis should be investigated in the future.