Abstract
The ability of horseradish peroxidase enzyme attached on three different reactor matrices: cellulose filter paper, nylon balls and nylon tubing, to remove 4-chlorophenol from aqueous solution is evaluated. The enzymatic reaction is extremely fast and the reaction products remained on the reactor matrix. Detachment or release of the reaction products from the reactor matrix is not observed. Results indicate that, over 80% removal efficiency can be obtained as long as enzyme activity is not limiting in the reactor. Systematic recycle batch reactor studies reveal that, initial reaction rates exhibit saturation with substrate concentration under conditions of excess peroxide. Inactivation of enzyme active sites by reaction intermediates is observed in the reactor studies. Immobilized peroxidase also catalyzes the oxidation of other chlorophenols and cresols.
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