Removal of dicofol from water by immobilized cellulase and its reaction kinetics.

Researches on the removal of dicofol catalyzed by immobilized cellulase were conducted. Factors, such as acidity, temperature, enzyme activity, and initial concentration of dicofol, which could influence the removal were studied. The optimal pH for dicofol removal by immobilized cellulase was approximately 4-7, broader than that for free enzymes. The removal efficiencies for immobilized and free cellulase both decreased with increasing initial concentration of dicofol. The K(m) for immobilized cellulase was slightly lower than that of free cellulase, suggesting that substrate affinity may be enhanced by immobilization. The optimum temperatures for immobilized and free cellulase were 45 °C and 50 °C. The removal reaction for immobilized cellulase was found to be a first-order reaction. The activation energy was 64.3 kJ mol(-1). The continuous oxidation of dicofol carried out in the static system of immobilized cellulase showed that the removal efficiency of immobilized cellulase remained after six cycles of operation. Thus, the catalytic efficiency of cellulase was improved greatly. As evidenced by infrared and gas chromatography-mass spectrometry data, the mechanism of reaction might involve an attack by the OH free radical of cellulase at a weak location of the dicofol molecule, resulting in the removal of three chlorine atoms from dicofol, thus oxygenizing dicofol and producing 4,4'-dichloro-dibenzophenone.