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

Arzu Ünal; Nazif Kolankaya; Abdurrahman Tanyolaç

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

2016

Arzu Ünal | Nazif Kolankaya | Abdurrahman Tanyolaç

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.

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