The comparative study of a laccase-natural clinoptilolite-based catalyst activity and free laccase activity on model compounds.

Abstract For the first time a laccase from Trametes versicolor was immobilized on a natural clinoptilolite with Si/Al = 5 to obtain a biocatalyst for environmental applications. Immobilization procedures exploiting adsorption and covalent binding were both tested, and only the last provided enough activity for practical applications. The optimal conditions for the immobilization of the enzyme on the support and the kinetic parameters for the free and covalent bonded laccase were determined. The laccase bonded to the zeolitic support showed a lower activity than the free laccase, but the pH and thermal stability were greater. 20 mg of dry biocatalyst containing 1 U of laccase were able to remove in 50 h 73–78% of 2-chlorophenol and 2,4-dichlorophenol in relatively concentrated aqueous solutions (100 μmol L −1 ).