This study was carried out to know the possibility of simultaneous utilization of laccase from white-rot fungus with cellulase on enzymatic hydrolysis of cellulosic substrate from autohydrolyzed oak wood. Laccases from 3 white-rot fungi, Pleurotus ostreatus. Ganoderma lucidum, and Phanerochaete chrysosporium, were isolated, purified and measured their activities. The highest activity was shown in Pleurotus ostreatus and the lowest in Phanerochaete chrysosporium. Laccase from Pleurotus ostreatus has optimum pH of 5.94, Km value of 3.209 mM and appeared to be stable at relatively wide pH range, 4.7-8.72. Temperature stability showed that 60% activity was preserved after 40 minutes at $50^{circ}C$. Laccase from Ganoderma lucidum reached to the maximum activity during 15-20 day incubation. This enzyme has optimum pH of 6.45, Km value of 6.71 mM and pH range of 5.0-9.0 for stabilization. 95% activity was preserved at $30^{circ}C$ and 58% activity at $50^{circ}C$. Concerned to the enzymatic hydrolysis of cellulosic substrate with both enzymes, cellulase and laccase, simultaneously, mixed culture filtrates and mycellium extracts were shown higher hydrolysis rates than those of Trichoderma viride. There were no significant differences in the extent of hydrolysis among various mixed culture filtrates and mycellium extracts.