Engineering synthetic bacterial consortia for enhanced desulfurization and revalorization of oil sulfur compounds
Autor: | Magdy El-Said Mohamed, Igor Martínez, Daniel Rozas, Eduardo Díaz, José Luis García |
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Přispěvatelé: | Saudi Aramco |
Rok vydání: | 2016 |
Předmět: |
0301 basic medicine
Microbial Consortia 030106 microbiology Synthetic bacterial consortia chemistry.chemical_element Bioengineering Biology Applied Microbiology and Biotechnology Metabolic engineering 03 medical and health sciences chemistry.chemical_compound 2-hydroxybiphenyll dsz cassettes Bioprocess chemistry.chemical_classification Sulfur Compounds Pseudomonas putida Rational design Monooxygenase biology.organism_classification Sulfur Enzyme Metabolic Engineering chemistry Biochemistry Dibenzothiophene Biotechnology |
Zdroj: | Digital.CSIC. Repositorio Institucional del CSIC instname |
ISSN: | 1096-7176 |
Popis: | 40 p.-7 fig.-1 tab. The 4S pathway is the most studied bioprocess for the removal of the recalcitrant sulfur of aromatic heterocycles present in fuels. It consists of three sequential functional units, encoded by the dszABCD genes, through which the model compound dibenzothiophene (DBT) is transformed into the sulfur-free 2-hydroxybiphenyl (2HBP) molecule. In this work, a set of synthetic dsz cassettes were implanted in Pseudomonas putida KT2440, a model bacterial “chassis” for metabolic engineering studies. The complete dszB1A1C1-D1 cassette behaved as an attractive alternative — to the previously constructed recombinant dsz cassettes — for the conversion of DBT into 2HBP. Refactoring the 4S pathway by the use of synthetic dsz modules encoding individual 4S pathway reactions revealed unanticipated traits, e.g., the 4S intermediate 2HBP-sulfinate (HBPS) behaves as an inhibitor of the Dsz monooxygenases, and once secreted from the cells it cannot be further taken up. That issue should be addressed for the rational design of more efficient biocatalysts for DBT bioconversions. In this sense, the construction of synthetic bacterial consortia to compartmentalize the 4S pathway into different cell factories for individual optimization was shown to enhance the conversion of DBT into 2HBP, overcome the inhibition of the Dsz enzymes by the 4S intermediates, and enable efficient production of unattainable high added value intermediates, e.g., HBPS, that are difficult to obtain using the current monocultures. This work has been supported by Saudi Aramco and by project DBR-001/08/WCOD. |
Databáze: | OpenAIRE |
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