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Kinetic model of laccase‐catalyzed oxidation of aqueous phenol
Author(s) -
Kurniawati Selvia,
Nicell James A.
Publication year - 2005
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.20497
Subject(s) - laccase , phenol , chemistry , catalysis , aqueous solution , substrate (aquarium) , oxygen , combinatorial chemistry , organic chemistry , enzyme , ecology , biology
Laccase from Trametes versicolor (EC 1.10.3.2) catalyzes the oxidation of aqueous phenol by oxygen and has demonstrated good potential for applications in various industrial and environmental processes. A kinetic model of this system has been developed to facilitate a better understanding of the mechanisms and rate‐limiting steps of enzyme‐catalyzed transformation and to eventually assist in the choice and design of suitable reactor systems. A kinetic model was derived based on the differential and mass balance equations that describe the interactions of various forms of the enzyme with the aromatic substrate and oxygen. This model also incorporated an expression accounting for enzyme inactivation over time due to the reaction environment. The model was validated by comparing model predictions with experimental observations of phenol transformation and oxygen consumption over time at a variety of enzyme concentrations. Excellent agreement was found between experimental data and predictions of the kinetic model. Sensitivity analyses demonstrated that the reaction between oxidized‐laccase and phenol was the rate‐limiting step. © 2005 Wiley Periodicals, Inc.