Mechanistic Distinction Between Oxidative and Chlorination Transformations of Chloroperoxidase from Caldariomyces fumago Demonstrated by Dye Decolorization

Effluents from the textile industry, particularly those containing synthetic azo dyes, poses a significant environmental threat, necessitating the development of more effective and sustainable pollutant removal methods. Traditional dye removal techniques often fall short in efficiency and environmental impact, prompting the exploration of enzymatic degradation as a promising alternative. This study focuses on chloroperoxidase, a natural biocatalyst recognized for its ability to oxidize synthetic dyes into less harmful products. By exploring the mechanistic distinction between chlorination and oxidative processes, we investigate the enzyme’s specific degradation pathways for azo dyes and the resulting by-products. Utilizing analytical techniques, including liquid chromatography/mass spectrometry (LC/MS), and density functional theory (DFT), we gain insights into the decolorization mechanism, revealing that the enzyme preferentially generates oxidative products through C–N bond cleavage as its initial degradation step. These findings underscore not only the unique mechanistic properties of chloroperoxidase but also its potential as a biocatalyst for industrial applications. This study advocates further research into the optimization of enzyme-based systems, highlighting their relevance in advancing greener chemical practices in the textile industry, thus contributing to more sustainable manufacturing processes.