Kinetic Modeling of Enzymatic Dechlorination of 2,4,6-Trichlorophenol with Laccase Enzyme obtained from white rot fungus Trametes versicolor

Abstract

This study examined kinetic modeling of the detoxification induced by dechlorination of laccase enzyme obtained from Trametes versicolor which is a white rot fungi strain and 2,4,6-trichlorophenol which is a toxic chlorinated phenolic compound. In the evaluation of the kinetics of detoxification induced by dechlorination of 2,4,6-trichlorophenol used as substrate, the Systat 10 software package which is a statistics program was used while two-substrate solution environment was used to explain the kinetic behavior of the dechlorination. It was observed as a result of experiments and statistical analysis that Moser equation is the optimal kinetic model. Given the statistical data obtained and the graph, the dual-substrate model was found to be compatible with the experimental data. The bio-kinetic parameter values obtained for the model that identifies enzymatic dechlorination kinetics were calculated as Vmax =9.341 ppmO2/min, Ks =38.254 g/L, Ko =20.747 ppm, R = 1.895 and N = 1.233. In the literature, no studies were found on kinetic modeling for the degradation of 2,4,6-trichlorophenol, and through this study, we have been first to conduct a study on kinetic modeling of the degradation induced by enzymatic dechlorination of 2,4,6-trichlorophenol. The GC/MS analysis results showed that the chlorophenolic compound used throughout the enzymatic dechlorination performed with laccase enzyme was degraded 80% to 100%. Based on the GC/MS analysis results, the conclusion that the enzyme responsible for the dechlorination was laccase was also found to support the findings available in literature.