Laccase was immobilized on MNH2SiO2 with glutaraldehyde as crosslinking agent.The effects on the activity of immobilized laccase,such as concentration of 2,4DCP (2,4dichlorophenols),acidity of solution,temperature were studied.The results show when concentration of 2,4DCP is 5 mg·L-1,pH of solution is 5.5,and the temperature is at 30℃,the highest removal rate of 2,4DCP is 42.28%.The results show that the optimal pH for immobilized laccase is higher than the best pH for free enzyme.Compared with the free enzyme,its stability and repetition are considerably improved.