Publications by authors named "Natividad Cabrera-Valladares"

The glycolytic intermediate phosphoenolpyruvate (PEP) is a precursor of several cellular components, including various aromatic compounds. Modifications to the PEP node such as PEP:sugar phosphotransferase system (PTS) or pyruvate kinase inactivation have been shown to have a positive effect on aromatics production capacity in Escherichia coli and Bacillus subtilis. In this study, pyruvate kinase and PTS-deficient B.

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The phosphoenolpyruvate (PEP) node is an important carbon distribution point in the central metabolic networks; therefore, its modification is a common strategy employed for developing microbial production strains. In this study, mutants of Bacillus subtilis 168 were generated with deletions of pykA (which encodes pyruvate kinase), ptsG (which encodes the glucose-specific IICBA(Glc) component) or the ptsGHI operon [which encodes IICBA(Glc), HPr protein and enzyme I from the PEP:sugar phosphotransferase system (PTS)]. These modifications caused a reduction in the initial rate of [(14)C]-glucose import, corresponding to 10.

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Article Synopsis
  • Anthranilate, an aromatic amine used in various industries, is typically synthesized through an unsustainable chemical process that relies on nonrenewable resources and creates toxic by-products.
  • Researchers modified a mutant strain of E. coli (W3110 trpD9923) to enhance its ability to produce anthranilate by using metabolic engineering techniques and identifying mutations affecting enzyme activity.
  • The best-performing engineered strains in laboratory experiments produced up to 0.75 g/L of anthranilate, while a more advanced fed-batch fermentation process achieved a significant production of 14 g/L within 34 hours, highlighting effective strategies for sustainable anthranilate biosynthesis.
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Pseudomonas aeruginosa produces the biosurfactants rhamnolipids and 3-(3-hydroxyalkanoyloxy)alkanoic acids (HAAs). In this study, we report the production of one family of rhamnolipids, specifically the monorhamnolipids, and of HAAs in a recombinant Escherichia coli strain expressing P. aeruginosa rhlAB operon.

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