MOnAm.tAD H. SIDDIQUE, CARL C. ST PIERRE
The study investigates the capability of horseradish peroxidase enzyme immobilized on three different reactor matrices: cellulose filter paper, nylon balls, and nylon tubing, to effectively remove 4-chlorophenol from aqueous solutions. The objective was to evaluate the efficiency of these immobilized enzymes in degrading this hazardous chemical, which poses significant environmental risks. Methodologically, the researchers conducted systematic recycle batch reactor studies to examine the enzymatic reaction speed and the effects of substrate concentration and peroxide on the reaction rates. Results revealed that with proper enzyme activity, over 80% removal efficiency could be achieved, while also indicating enzyme inactivation due to reaction intermediates. The immobilized peroxidase also demonstrated capacity to catalyze the oxidation of other chlorophenols and cresols. This work contributes to understanding the potential of enzyme immobilization in hazardous waste treatment applications.
@article{bb8d3537-66fb-4812-a113-fab13de9ed4f,
title={Immobilized enzyme catalyzed removal of},
author={MOnAm.tAD H. SIDDIQUE and CARL C. ST PIERRE},
year={2026},
language={en}
}TY - JOUR TI - Immobilized enzyme catalyzed removal of AU - MOnAm.tAD H. SIDDIQUE AU - CARL C. ST PIERRE PY - 2026 LA - en ER -
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