Degradation of 2-chlorophenol by laccase-zeolite biocatalyst

Degradation of 2-chlorophenol was studied using a laccase-based catalyst immobilized, for the first time, with a natural clinoptilolite as solid support. The optimal conditions for the enzyme immobilization were determined together with pH and temperature stability. The biocatalyst containing 1 U of laccase was able to remove 0.73 micromoles di 2-chlorophenol.