LAUSR

The phenolic compound catechol has found various applications in the industry but is often discharged untreated in industrial effluents. Catechol is highly toxic and adversely affects the environment. This has increased extensive investigation into elucidating the effects of various synthetic elements or different biocatalysts on catechol, thereby leading the way to its bioremediation. Hence, an electrochemical-based study on catechol in the presence of the enzyme laccase could provide a basic understanding of the unique characteristics exhibited by catechol, thus facilitating a distinct perspective to its subsequent treatment and removal. The present study focuses on the electrochemical characterization of catechol based on the oxidation of laccase and the redox mediator 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS). Catechol exhibited distinct electrochemical behavior across various concentrations. The unique electroactive nature of ABTS assisted in the polymerization of catechol which was found to be concentration-dependent. Laccase produced a higher oxidation-reduction rate, thereby producing a much more stable condition for the polymerization of catechol. However, with the laccase-mediator system (LMS), the catechol polymerization rate was distinctly higher and more gradual with the enzyme utilizing the electroactive species produced by ABTS to increase the electron transfer and producing a combinatorial impact on the phenolic compound. This study could rightly serve as the building block in developing future technologies like wastewater treatment and biosensors for catechol bioremediation.