In the process of lignocellulose conversion to ethanol by enzymatic saccharification and fermentation, unproductive adsorption of cellulase on lignin is one of the key inhibitory factors for the saccharification process. In this study we prepared purified milled wood lignin from softwood Cryptomeria japonica and hardwood Eucalyptus globulus to elucidate the behavior of adsorption and desorption of cellulase components on lignin. A commercial cellulase cocktail from Trichoderma reesei (Accellerase 1500) was used to investigate the affinity of cellulase components on the isolated lignin. β-glucosidase showed high affinity for the isolated lignin, whereas CBH I exhibited higher desorptive properties than those of the other enzyme components.