A major problem in the enzymatic hydrolysis of lignocellulosic substrates is the very strong bonding of cellulase to lignin and even cellulose in the hydrolysis residues. This phenomenon inhibits recycle of the cellulase which is a major expense of the enzymatic hydrolysis process. In this paper, autohydrolyzed wood was delignified by two-stage with a 0.3% Na OH extraction and oxygen-alkali bleaching and was subjected to enzymatic hydrolysis with cellulase. Also, an improved almost quantitative recycle process of cellulase enzyme was discussed. In enzyme recovery by affinity method. the first recycling showed relatively high hydrolysis rate of 97.4%. Even at the third recycle. hydrolysis rate was 86.7 percents. In the case of cellulase recovery by ultrafiltration method, first 2 recycling treatments resulted very high hydrolysis rate(97.0-97.7%). Even the third recycling showed about 94.2%. Authoydrolysis of oak wood followed by 2-stage delignification with alkali and oxygen-alkali produced a substrate for enzymatic hydrolysis that allowed almost quantitative recycle of cellulase.