Biodesulfurization enhancement via targeted re-insertion of the flavin reductase dszD in the genome of the model strain Rhodococcus qingshengii IGTS8
Biodesulfurization (BDS) has emerged as an alternative to the excessively costly hydrodesulfurization of recalcitrant heterocyclic sulfur compounds, such as dibenzothiophene (DBT) and its derivatives. The model desulfurizing strain Rhodococcus qingshengii IGTS8 is responsible for the removal of sulf...
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Elsevier
2025-01-01
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author | Olga Martzoukou Fotios Klenias Eleni Kopsini Dimitris G. Hatzinikolaou |
author_facet | Olga Martzoukou Fotios Klenias Eleni Kopsini Dimitris G. Hatzinikolaou |
author_sort | Olga Martzoukou |
collection | DOAJ |
description | Biodesulfurization (BDS) has emerged as an alternative to the excessively costly hydrodesulfurization of recalcitrant heterocyclic sulfur compounds, such as dibenzothiophene (DBT) and its derivatives. The model desulfurizing strain Rhodococcus qingshengii IGTS8 is responsible for the removal of sulfur through the 4S metabolic pathway, operating through a plasmid-borne dszABC operon, as well as the chromosomal gene for the flavin reductase, dszD. However, naturally occurring biocatalysts do not exhibit the required BDS activity to be useful for industrial applications and for this reason, genetic modifications are currently being explored. Here, we constructed a genetically modified R. qingshengii IGTS8 strain, which carries an additional copy of the flavin reductase gene dszD under the control of the rhodococcal promoter Pkap1, inserted in the neutral chromosomal genetic locus crtI. We conducted a comparative study of the growth and biodesulfurization capabilities of Pkap1-dszD, wild-type and crtIΔ strains, grown on different types and concentrations of carbon and sulfur sources. A significant enhancement of biodesulfurization activity, maximum calculated biomass, and dszD transcript levels in the presence of DBT as the sole sulfur source was achieved for the Pkap1-dszD strain paving the way for further studies that could lead to a more viable commercial biodesulfurization process. |
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id | doaj-art-21c268654b4a48ae973397ca8e518bed |
institution | Kabale University |
issn | 2405-8440 |
language | English |
publishDate | 2025-01-01 |
publisher | Elsevier |
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series | Heliyon |
spelling | doaj-art-21c268654b4a48ae973397ca8e518bed2025-02-02T05:28:30ZengElsevierHeliyon2405-84402025-01-01112e41899Biodesulfurization enhancement via targeted re-insertion of the flavin reductase dszD in the genome of the model strain Rhodococcus qingshengii IGTS8Olga Martzoukou0Fotios Klenias1Eleni Kopsini2Dimitris G. Hatzinikolaou3Enzyme and Microbial Biotechnology Unit, Department of Biology, National and Kapodistrian University of Athens, Athens, GreeceEnzyme and Microbial Biotechnology Unit, Department of Biology, National and Kapodistrian University of Athens, Athens, GreeceEnzyme and Microbial Biotechnology Unit, Department of Biology, National and Kapodistrian University of Athens, Athens, GreeceCorresponding author.; Enzyme and Microbial Biotechnology Unit, Department of Biology, National and Kapodistrian University of Athens, Athens, GreeceBiodesulfurization (BDS) has emerged as an alternative to the excessively costly hydrodesulfurization of recalcitrant heterocyclic sulfur compounds, such as dibenzothiophene (DBT) and its derivatives. The model desulfurizing strain Rhodococcus qingshengii IGTS8 is responsible for the removal of sulfur through the 4S metabolic pathway, operating through a plasmid-borne dszABC operon, as well as the chromosomal gene for the flavin reductase, dszD. However, naturally occurring biocatalysts do not exhibit the required BDS activity to be useful for industrial applications and for this reason, genetic modifications are currently being explored. Here, we constructed a genetically modified R. qingshengii IGTS8 strain, which carries an additional copy of the flavin reductase gene dszD under the control of the rhodococcal promoter Pkap1, inserted in the neutral chromosomal genetic locus crtI. We conducted a comparative study of the growth and biodesulfurization capabilities of Pkap1-dszD, wild-type and crtIΔ strains, grown on different types and concentrations of carbon and sulfur sources. A significant enhancement of biodesulfurization activity, maximum calculated biomass, and dszD transcript levels in the presence of DBT as the sole sulfur source was achieved for the Pkap1-dszD strain paving the way for further studies that could lead to a more viable commercial biodesulfurization process.http://www.sciencedirect.com/science/article/pii/S2405844025002798BiodesulfurizationFMN reductaseDibenzothiopheneGenetic engineeringModel biocatalystActinomycetes |
spellingShingle | Olga Martzoukou Fotios Klenias Eleni Kopsini Dimitris G. Hatzinikolaou Biodesulfurization enhancement via targeted re-insertion of the flavin reductase dszD in the genome of the model strain Rhodococcus qingshengii IGTS8 Heliyon Biodesulfurization FMN reductase Dibenzothiophene Genetic engineering Model biocatalyst Actinomycetes |
title | Biodesulfurization enhancement via targeted re-insertion of the flavin reductase dszD in the genome of the model strain Rhodococcus qingshengii IGTS8 |
title_full | Biodesulfurization enhancement via targeted re-insertion of the flavin reductase dszD in the genome of the model strain Rhodococcus qingshengii IGTS8 |
title_fullStr | Biodesulfurization enhancement via targeted re-insertion of the flavin reductase dszD in the genome of the model strain Rhodococcus qingshengii IGTS8 |
title_full_unstemmed | Biodesulfurization enhancement via targeted re-insertion of the flavin reductase dszD in the genome of the model strain Rhodococcus qingshengii IGTS8 |
title_short | Biodesulfurization enhancement via targeted re-insertion of the flavin reductase dszD in the genome of the model strain Rhodococcus qingshengii IGTS8 |
title_sort | biodesulfurization enhancement via targeted re insertion of the flavin reductase dszd in the genome of the model strain rhodococcus qingshengii igts8 |
topic | Biodesulfurization FMN reductase Dibenzothiophene Genetic engineering Model biocatalyst Actinomycetes |
url | http://www.sciencedirect.com/science/article/pii/S2405844025002798 |
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