Removal of 2,4-dichlorophenol (2,4-DCP) by TiO 2/UV photocatalytic, laccase, and simultaneous photocatalytic-enzymatic treatments were investigated. Coupling of native laccase with TiO 2/UV showed a negative synergetic effect due to the rapid inactivation of laccase. Immobilizing laccase covalently to controlled porous glass (CPG) effectively enhanced the stability of laccase against TiO 2/UV induced inactivation. By coupling CPG-laccase with the TiO 2/UV the degradation efficiency of 2,4-DCP was significantly increased as compared with the results obtained when immobilized laccase or TiO 2/UV were separately used. Moreover, the enhancement was more remarkable for the degradation of 2,4-DCP with high concentration, such that for the degradation of 5mM 2,4-DCP, 90% removal percentage was achieved within 2h with the coupled degradation process. While for the TiO 2/UV and CPG-laccase process, the removal percentage of 2,4-DCP at 2h were only 26.5% and 78.1%, respectively. The degradation kinetics were analyzed using a intermediate model by taking into account of the intermediates formed during the degradation of 2,4-DCP. The high efficiency of the coupled degradation process therefore provided a novel strategy for degradation of concentrated 2,4-DCP. Furthermore, a thermometric biosensor using the immobilized laccase as biorecognition element was constructed for monitoring the degradation of 2,4-DCP, the result indicated that the biosensor was precise and sensitive.
|Original language||English (US)|
|Number of pages||6|
|Journal||Journal of Hazardous Materials|
|State||Published - Feb 29 2012|
Bibliographical noteFunding Information:
The project is supported by grants from National Natural Science Foundation of China (# 20728607 , 20706054 , 20976180 ), and 973 Program ( 2009CB724705 ). This work is also sponsored by the Scientific Research Foundation for the Returned Overseas Chinese Scholars, State Education Ministry (No. 2006-331 ). Dr. B. Danielsson of Lund University, Sweden is greatly acknowledged for providing the enzyme thermistor.