Efficient degradation of various emerging pollutants by wild type and evolved fungal DyP4 peroxidases.
The accumulation of emerging pollutants in the environment remains a major concern as evidenced by the increasing number of reports citing their potential risk on environment and health. Hence, removal strategies of such pollutants remain an active area of investigation. One way through which emergi...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2022-01-01
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| Series: | PLoS ONE |
| Online Access: | https://doi.org/10.1371/journal.pone.0262492 |
| _version_ | 1819289106693226496 |
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| author | Khawlah Athamneh Aysha Alneyadi Aya Alsadik Tuck Seng Wong Syed Salman Ashraf |
| author_facet | Khawlah Athamneh Aysha Alneyadi Aya Alsadik Tuck Seng Wong Syed Salman Ashraf |
| author_sort | Khawlah Athamneh |
| collection | DOAJ |
| description | The accumulation of emerging pollutants in the environment remains a major concern as evidenced by the increasing number of reports citing their potential risk on environment and health. Hence, removal strategies of such pollutants remain an active area of investigation. One way through which emerging pollutants can be eliminated from the environment is by enzyme-mediated bioremediation. Enzyme-based degradation can be further enhanced via advanced protein engineering approaches. In the present study a sensitive and robust bioanalytical liquid chromatography-tandem mass spectrometry (LCMSMS)-based approach was used to investigate the ability of a fungal dye decolorizing peroxidase 4 (DyP4) and two of its evolved variants-that were previously shown to be H2O2 tolerant-to degrade a panel of 15 different emerging pollutants. Additionally, the role of a redox mediator was examined in these enzymatic degradation reactions. Our results show that three emerging pollutants (2-mercaptobenzothiazole (MBT), paracetamol, and furosemide) were efficiently degraded by DyP4. Addition of the redox mediator had a synergistic effect as it enabled complete degradation of three more emerging pollutants (methyl paraben, sulfamethoxazole and salicylic acid) and dramatically reduced the time needed for the complete degradation of MBT, paracetamol, and furosemide. Further investigation was carried out using pure MBT to study its degradation by DyP4. Five potential transformation products were generated during the enzymatic degradation of MBT, which were previously reported to be produced during different bioremediation approaches. The current study provides the first instance of the application of fungal DyP4 peroxidases in bioremediation of emerging pollutants. |
| first_indexed | 2024-12-24T03:01:35Z |
| format | Article |
| id | doaj.art-0f59dcbf2f564fd3b840249d1d228b12 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-24T03:01:35Z |
| publishDate | 2022-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-0f59dcbf2f564fd3b840249d1d228b122022-12-21T17:18:11ZengPublic Library of Science (PLoS)PLoS ONE1932-62032022-01-01171e026249210.1371/journal.pone.0262492Efficient degradation of various emerging pollutants by wild type and evolved fungal DyP4 peroxidases.Khawlah AthamnehAysha AlneyadiAya AlsadikTuck Seng WongSyed Salman AshrafThe accumulation of emerging pollutants in the environment remains a major concern as evidenced by the increasing number of reports citing their potential risk on environment and health. Hence, removal strategies of such pollutants remain an active area of investigation. One way through which emerging pollutants can be eliminated from the environment is by enzyme-mediated bioremediation. Enzyme-based degradation can be further enhanced via advanced protein engineering approaches. In the present study a sensitive and robust bioanalytical liquid chromatography-tandem mass spectrometry (LCMSMS)-based approach was used to investigate the ability of a fungal dye decolorizing peroxidase 4 (DyP4) and two of its evolved variants-that were previously shown to be H2O2 tolerant-to degrade a panel of 15 different emerging pollutants. Additionally, the role of a redox mediator was examined in these enzymatic degradation reactions. Our results show that three emerging pollutants (2-mercaptobenzothiazole (MBT), paracetamol, and furosemide) were efficiently degraded by DyP4. Addition of the redox mediator had a synergistic effect as it enabled complete degradation of three more emerging pollutants (methyl paraben, sulfamethoxazole and salicylic acid) and dramatically reduced the time needed for the complete degradation of MBT, paracetamol, and furosemide. Further investigation was carried out using pure MBT to study its degradation by DyP4. Five potential transformation products were generated during the enzymatic degradation of MBT, which were previously reported to be produced during different bioremediation approaches. The current study provides the first instance of the application of fungal DyP4 peroxidases in bioremediation of emerging pollutants.https://doi.org/10.1371/journal.pone.0262492 |
| spellingShingle | Khawlah Athamneh Aysha Alneyadi Aya Alsadik Tuck Seng Wong Syed Salman Ashraf Efficient degradation of various emerging pollutants by wild type and evolved fungal DyP4 peroxidases. PLoS ONE |
| title | Efficient degradation of various emerging pollutants by wild type and evolved fungal DyP4 peroxidases. |
| title_full | Efficient degradation of various emerging pollutants by wild type and evolved fungal DyP4 peroxidases. |
| title_fullStr | Efficient degradation of various emerging pollutants by wild type and evolved fungal DyP4 peroxidases. |
| title_full_unstemmed | Efficient degradation of various emerging pollutants by wild type and evolved fungal DyP4 peroxidases. |
| title_short | Efficient degradation of various emerging pollutants by wild type and evolved fungal DyP4 peroxidases. |
| title_sort | efficient degradation of various emerging pollutants by wild type and evolved fungal dyp4 peroxidases |
| url | https://doi.org/10.1371/journal.pone.0262492 |
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