Engineering of Corynebacterium glutamicum for growth and succinate production from levoglucosan as a pyrolytic sugar substrate
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ABSTRACT:
ORGANISM(S): Corynebacterium glutamicum
PROVIDER: GSE68483 | GEO | 2016/03/17
SECONDARY ACCESSION(S): PRJNA282908
REPOSITORIES: GEO
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Project description:Metabolically engineered Corynebacterium glutamicum strains were constructed for the enhanced production of L-arginine, and their gene expression profiles were investigated Gene expression profiles of two C. glutamicum strains AR2 and AR6 were examined for the 3043 genes twice.
2013-11-26 | E-GEOD-52737 | biostudies-arrayexpress
Project description:Metabolically engineered Corynebacterium glutamicum strains were constructed for the enhanced production of L-arginine, and their gene expression profiles were investigated
2013-11-26 | GSE52737 | GEO
Project description:Efficient assimilation of renewable feedstocks is the cornerstone for achieving sustainable and economical microbial production of commodity chemicals. Unfortunately, most renewables are foreign to the cellular metabolism of classical industrial workhorses, resulting in unsatisfactory biomanufacturing performance. Here, Corynebacterium glutamicum was systematically engineered for rapid non-natural xylose metabolism and the underlying adaptations were elucidated by combining metabolic engineering, adaptive laboratory evolution and systems biology techniques. A plasmid-free, stable and efficient xylose-utilizing chassis strain, named CGS15, was reconstructed with both a rapid specific growth rate of 0.341 h-1 on xylose and an excellent co-utilization of glucose and xylose at a ratio of about 2:1. For the first time, we revealed a novel xylose regulatory mechanism by the endogenous transcription factor IpsA with global regulatory effects on C. glutamicum core carbon and energy metabolism. The coordination between the heterologous xylose metabolism and the endogenous carbon/energy metabolism both endowed cells with accelerated growth and released carbon catabolite repression. Finally, this chassis demonstrated great promise for lignocellulosic biorefinery applications by producing 97.1 g/L of the platform compound succinate from corn stalk hydrolysate with an average productivity of 8.09 g/L/h. This work provides an elegant paradigm to understand and engineer the metabolism of renewable substrates for sustainable biomanufacturing.
2022-10-03 | GSE184402 | GEO
Project description:The Gram-positive soil bacterium Corynebacterium glutamicum is widely used in industrial fermentative processes for the production of amino acids. The world production of L-lysine has surpassed 2 million tons per year. Glucose is taken up into the C. glutamicum cell by the phosphotransferase system PTS which can be replaced and/or enhanced by a permease and a glucokinase. Heterologous expression of the gene for the high-affinity glucose permease from Streptomyces coelicolor and of the Bacillus subitilis glucokinase gene fully compensated for the absence of the PTS in hpr strains and strains grew as fast with glucose as C. glutamicum wild type. Growth of PTS-positive strains with glucose was accelerated when the endogenous inositol permease IolT2 and the glucokinase from Bacillus subtilis were overproduced using plasmid pEKEx3-IolTBest. When the genome-reduced C. glutamicum strain GRLys1 carrying additional in-frame deletions of sugR and ldhA to derepress glycolytic and PTS genes and to circumvent formation of L-lactate as by-product was transformed with this plasmid, a 40% higher L-lysine titer and a 30% higher volumetric productivity as compared to GRLys1(pEKEx3) resulted. The non-proteinogenic amino acid pipecolic acid (L-PA), a precursor of immunosuppressants, peptide antibiotics or piperidine alkaloids, can be derived from L-lysine. To enable production of L-PA by the L-lysine producing strain, the L-Lysine dehydrogenase gene lysDH from Silicibacter pomeroyi and the endogenous pyrroline 5-carboxylate reductase gene proC were expressed as synthetic operon. This enabled C. glutamicum to L-PA with a yield of 0.49 ± 0.03 gg-1 and a volumetric productivity of 0.04 ± 0.00 gL-1h-1.To the best of our knowledge, this is the first fermentative process for the production of L-PA.
2016-03-30 | GSE79690 | GEO
Project description:The Gram-positive soil bacterium Corynebacterium glutamicum is widely used in industrial fermentative processes for the production of amino acids. The world production of L-lysine has surpassed 2 million tons per year. Glucose is taken up into the C. glutamicum cell by the phosphotransferase system PTS which can be replaced and/or enhanced by a permease and a glucokinase. Heterologous expression of the gene for the high-affinity glucose permease from Streptomyces coelicolor and of the Bacillus subitilis glucokinase gene fully compensated for the absence of the PTS in ï??hpr strains and strains grew as fast with glucose as C. glutamicum wild type. Growth of PTS-positive strains with glucose was accelerated when the endogenous inositol permease IolT2 and the glucokinase from Bacillus subtilis were overproduced using plasmid pEKEx3-IolTBest. When the genome-reduced C. glutamicum strain GRLys1 carrying additional in-frame deletions of sugR and ldhA to derepress glycolytic and PTS genes and to circumvent formation of L-lactate as by-product was transformed with this plasmid, a 40% higher L-lysine titer and a 30% higher volumetric productivity as compared to GRLys1(pEKEx3) resulted. The non-proteinogenic amino acid pipecolic acid (L-PA), a precursor of immunosuppressants, peptide antibiotics or piperidine alkaloids, can be derived from L-lysine. To enable production of L-PA by the L-lysine producing strain, the L-Lysine dehydrogenase gene lysDH from Silicibacter pomeroyi and the endogenous pyrroline 5-carboxylate reductase gene proC were expressed as synthetic operon. This enabled C. glutamicum to L-PA with a yield of 0.49 ± 0.03 gg-1 and a volumetric productivity of 0.04 ± 0.00 gL-1h-1.To the best of our knowledge, this is the first fermentative process for the production of L-PA. Two conditions tested, 200 mM NaCl Vs 200 mM pipecolic supplemented in the culture medium, control experiments done with the addition of 200mM of NaCl. Four technical replicates.
2016-03-30 | E-GEOD-79690 | biostudies-arrayexpress
Project description:Transcriptional profiling of C. glutamicum wild-type and mutant strains grown under different conditions.
2022-07-22 | GSE169361 | GEO
Project description:Transcriptional profiling of C. glutamicum wild-type and mutant strains grown under different conditions.
2022-07-22 | GSE171301 | GEO
Project description:Strains: non-producing refernece strain pXMJ19 (CR099 pXMJ19; Goldbeck et al., 2021) and Pediocin-producer pxMJ19 ped (CR099 pXMJ19 Ptac pedACDCg, Goldbeck et al., 2021) Pediocin-producing and non-producing strains of Corynebacterium glutamicum were compared in a whole genome microarray analysis setup in order to identify potential strain optimization targets
2023-03-08 | GSE220713 | GEO
Project description:Ciprofloxacin, an inhibitor of bacterial gyrase and topoisomerase IV, was shown to inhibit growth of C. glutamicum with concomitant excretion of L-glutamate. C. glutamicum strains overproducing L-lysine, L-arginine, L-ornithine, and putrescine, respectively, produced L-glutamate instead of the desired amino acid when exposed to ciprofloxacin. Even in the absence of the putative L-glutamate exporter gene yggB, ciprofloxacin effectively triggered L-glutamate production. When C. glutamicum wild type was cultivated under nitrogen-limiting conditions, 2-oxoglutarate rather than L-glutamate was produced as consequence of exposure to ciprofloxacin. Transcriptome analysis revealed that ciprofloxacin increased RNA levels of genes involved in DNA synthesis, repair and modification. Enzyme assays showed that 2-oxoglutarate dehydrogenase activity was decreased due to ciprofloxacin addition. Here, it was shown for the first time that production of L-glutamate by C. glutamicum may be triggered by an inhibitor of DNA synthesis and L-glutamate titers of up to 37 ± 1 mM and a substrate specific L-glutamate yield of 0.13 g/g were reached.
2016-01-26 | GSE77189 | GEO
Project description:The dicarboxylic acid glutarate is gaining attention in the chemical and pharmaceutical industry as promising building-block. Synthesis of glutarate via microbial fermentation is a desirable aim which will allow the production of biopolymers avoiding fossil raw materials. Here, by rational metabolic engineering of the biofactory microorganism Corynebacterium glutamicum the fermentative production of glutarate from glucose was established. Modifications focused on increase glucose consumption and reduce by-products formation together with the heterologous overexpression of the L-lysine decarboxylase, putrescine transaminase and putrescine dehydrogenase genes from E. coli in the L-lysine producer GRLys1 allowed production the glutarate precursor 5-aminovalerate. Additional heterologous overexpression of 5-aminovalerate amino transferase and glutarate-semialdehyde dehydrogenase genes from C. glutamicum and three Pseudomonas species enabled glutarate synthesis from glucose. By coupling glutarate production with the glutamate synthesis of C. glutamicum glutarate titer improved 10%. The final strain was tested in a glucose-based fed-batch fermentation
2018-11-20 | GSE117175 | GEO