Combined experimental and theoretical study on the removal of pollutant compounds by peroxidases: affinity and reactivity toward a bioremediation catalyst
Language English Country England, Great Britain Media print-electronic
Document type Journal Article
- Keywords
- HRP, experimental techniques, pollutant, soybean peroxidase, theoretical calculations,
- MeSH
- Biodegradation, Environmental * MeSH
- Bromphenol Blue chemistry MeSH
- Catalytic Domain MeSH
- Catalysis MeSH
- Kinetics MeSH
- Coumaric Acids chemistry MeSH
- Environmental Pollutants * chemistry MeSH
- Molecular Conformation MeSH
- Models, Molecular MeSH
- Oxidation-Reduction MeSH
- Peroxidases * chemistry metabolism MeSH
- Molecular Docking Simulation MeSH
- Substrate Specificity MeSH
- Models, Theoretical * MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Hydrogen Bonding MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Bromphenol Blue MeSH
- ferulic acid MeSH Browser
- Coumaric Acids MeSH
- Environmental Pollutants * MeSH
- Peroxidases * MeSH
Water pollution is a significant and growing problem throughout the world, especially in developing countries. In order to minimize environmental problems, catalysts have increasingly been designed to remove pollutants from the water. In an attempt to innovate by the creation of new low-cost alternatives to efficiently remove pollutants, the enzymatic treatment has been intensely studied for this purpose. Reactions catalyzed by enzymes are able to perform specific treatments, commonly with high rates of the final products. With this, the enzyme, peroxidase, is a promising candidate as a bioremediation catalyst. The efficiency of oxidoreductive enzymes, such as horseradish peroxidase (HRP) and soybean peroxidase (SP) have been studied, given that their performance depends on the substrate. In this investigation, experimental techniques and theoretical calculations have been employed in order to investigate the oxidative process for the ferulic acid and bromophenol blue dyes, performed by HRP and SP. Both enzymes showed a comparable behavior with respect to ferulic acid substrate. On the other hand, by utilizing bromophenol blue dye as a substrate, the behavior of the employed catalysts was significantly different. Experimental data have shown that HRP was more active toward bromophenol blue when compared to ferulic acid, being more rapidly degraded by the HRP enzyme. This tendency was confirmed by our theoretical docking, PM6 semi-empirical method, and DFT calculation results, in which the interaction, binding energies, and transition states were determined.
b Department of Chemistry Federal University of Lavras 37200 000 Lavras Brazil
c Center for Basic and Applied Research University Hradec Kralove Hradec Kralove Czech Republic
Department of Chemistry Federal University of Minas Gerais 31270 901 Belo Horizonte Brazil
References provided by Crossref.org
