Abstract: Two active components Eg1 and Eg2 of β-endoglucanase were purified by utilizing salting out,Sephadex G-75 chromatography and DEAE-Sephadex A50 chromatography from the fermentation broth of Trichoderma reesei QM9414.The relative molecular weights of Eg1 and Eg2 were 65.47ku and 57.04ku respectively;The optimal temperatures of Eg1 and Eg2 were 50℃ and 55℃ respectively;the optimal pHwas 4.8 and 5.0 and their Michaelis constants were Km=3.76×10-2g/Land Km=4.20×10-2g/L.According to their enzymological characters,they are newly discovered.It seemed that the research built a basis for the further study of β-endoglucanase in T.reesei QM9414.