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Kinetics of horseradish peroxidase‐catalysed polymerization and precipitation of aqueous 4‐chlorophenol
Author(s) -
Nicell James A.
Publication year - 1994
Publication title -
journal of chemical technology and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.64
H-Index - 117
eISSN - 1097-4660
pISSN - 0268-2575
DOI - 10.1002/jctb.280600214
Subject(s) - horseradish peroxidase , hydrogen peroxide , aqueous solution , chemistry , polymerization , steady state (chemistry) , precipitation polymerization , kinetics , precipitation , peroxidase , transient (computer programming) , transient state , chemical engineering , organic chemistry , computer science , radical polymerization , polymer , physics , operating system , quantum mechanics , meteorology , electrical engineering , enzyme , engineering
Hydrogen‐peroxide oxidoreductase (EC 1.11.1.7) from horseradishes catalyzes the polymerization and precipitation of aromatic compounds from aqueous solutions in the presence of hydrogen peroxide. This process has demonstrated good potential as a technique for the removal of toxic contaminants from wastewaters. Steady‐state, fully transient and pseudo‐steady‐state models of the horseradish peroxidase system have been developed to assist in the under‐standing of the dominant mechanisms of inactivation and to aid in the selection and design of an appropriate reactor system. Model validation was performed by comparing model predictions with experimental observations of the polymerization and precipitation of 4‐chlorophenol. Good agreement was found between experimental data and predictions of the fully transient and pseudo‐steady‐state models. The pseudo‐steady‐state model has the advantage of reduced complexity with a corresponding reduction in computation time required to solve model equations while maintaining the predictive ability of the fully transient model.