RESUMO
The aim of this study was to investigate the bioremediation potential of polychlorinated biphenyls (PCBs) in soil, mimicking three strategies: (a) mycoaugmentation: by the addition of Trametes sanguinea and Pleurotus sajor-caju co-cultures immobilized on sugarcane bagasse; (b) biostimulation: by supplementation of sugarcane bagasse; and (c) natural attenuation: no amendments. The experiments were done in microcosms using Ultisol soil. Remediation effectiveness was assessed based on pollutants content, soil characteristics, and ecotoxicological tests. Biostimulation and mycoaugmentation demonstrated the highest PCBs-removal (approx. 90%) with a significant toxicity reduction at 90 d. The studied strains were able to survive during the incubation period in non-sterilized soil. Laccase, manganese-peroxidase and endoxylanase activities increased significantly in co-cultures after 60 d. Sugarcane bagasse demonstrated to be not only a suitable support for fungal immobilization but also an efficient substrate for fungal colonization of PCBs-contaminated soils. Mycoaugmentation and biostimulation with sugarcane bagasse improved oxidable organic matter and phosphorous contents as well as dehydrogenase activity in soil. Therefore, biostimulation with sugarcane bagasse and mycoaugmentation applying dual white-rot fungal cultures constitute two efficient bioremediation alternatives to restore PCBs-contaminated soils.
Assuntos
Biodegradação Ambiental , Poluentes do Solo/metabolismo , Celulose , Ecotoxicologia , Lacase , Peroxidases , Fósforo , Bifenilos Policlorados , Saccharum , Solo/química , Microbiologia do Solo , Poluentes do Solo/análise , TrametesRESUMO
Abstract Oxidative enzymes secreted by white rot fungi can be applied in several technological processes within the paper industry, biofuel production and bioremediation. The discovery of native strains from the biodiverse Misiones (Argentina) forest can provide useful enzymes for biotechnological purposes. In this work, we evaluated the laccase and manganese peroxidase secretion abilities of four newly discovered strains of Trametes sp. that are native to Misiones. In addition, the copper response and optimal pH and temperature for laccase activity in culture supernatants were determined.The selected strains produced variable amounts of laccase and MnP; when Cu2+ was added, both enzymes were significantly increased. Zymograms showed that two isoenzymes were increased in all strains in the presence of Cu2+. Strain B showed the greatest response to Cu2+ addition, whereas strain A was more stable at the optimal temperature and pH. Strain A showed interesting potential for future biotechnological approaches due to the superior thermo-stability of its secreted enzymes.
Assuntos
Proteínas Fúngicas/metabolismo , Lacase/metabolismo , Trametes/enzimologia , Argentina , Temperatura , Estabilidade Enzimática , Proteínas Fúngicas/genética , Proteínas Fúngicas/química , Lacase/genética , Lacase/química , Trametes/isolamento & purificação , Trametes/genéticaRESUMO
Oxidative enzymes secreted by white rot fungi can be applied in several technological processes within the paper industry, biofuel production and bioremediation. The discovery of native strains from the biodiverse Misiones (Argentina) forest can provide useful enzymes for biotechnological purposes. In this work, we evaluated the laccase and manganese peroxidase secretion abilities of four newly discovered strains of Trametes sp. that are native to Misiones. In addition, the copper response and optimal pH and temperature for laccase activity in culture supernatants were determined. The selected strains produced variable amounts of laccase and MnP; when Cu(2+) was added, both enzymes were significantly increased. Zymograms showed that two isoenzymes were increased in all strains in the presence of Cu(2+). Strain B showed the greatest response to Cu(2+) addition, whereas strain A was more stable at the optimal temperature and pH. Strain A showed interesting potential for future biotechnological approaches due to the superior thermo-stability of its secreted enzymes.