A new type of biocatalyst was developed to facilitate the biochemical decomposition of 4-chlorophenol. Oxydoreductases that catalyze the initial 4-chlorophenol (4-CP) biodegradation steps were prepared by recombinant technique and then they were immobilized onto inorganic enzyme support, zeolite. It was extracted from coal fly ash and coated with Nickel ion(Ⅱ), which promoted a favorable metal-histidine binding between enzyme support and enzymes. Monooxygenase (CphC-I), dioxygenase (CphA-I), and flavin reductase (Fre) were cloned and overexpressed from a 4-CP degrading bacterium, Pseudarthrobacter chlorophenolicus A6, and Escherichia coli K-12, respectively. Histidine was expressed in all enzymes.  This biocatalyst is expected to provide useful information on the development of a new enzymatic treatment of phenolic hydrocarbon contaminants. 

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