ArticleMicrobial cell factories2016
Systematic manipulation of glutathione metabolism in Escherichia coli for improved glutathione production.
Article in Microbial cell factories, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 40 citations in OpenAlex.
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- Bioprocess optimization of glutathione production by Saccharomyces boulardii: biochemical characterization of glutathione peroxidase.Archives of microbiology · 2021Article
- A Nitrogen Metabolic Enzyme ProvidesACS infectious diseases · 2021Article
- Efficient production of glutathione with multi-pathway engineering in Corynebacterium glutamicum.Journal of industrial microbiology & biotechnology · 2019Article
- Metabolic engineering of Lactococcus lactis for high level accumulation of glutathione and S-adenosyl-L-methionine.World journal of microbiology & biotechnology · 2019Article
- Regulation of ATP levels in Escherichia coli using CRISPR interference for enhanced pinocembrin production.Microbial cell factories · 2018Article
- Production of Ophthalmic Acid Using Engineered Escherichia coli.Applied and environmental microbiology · 2018Article
- Acrolein-stressed threshold adaptation alters the molecular and metabolic bases of an engineered Saccharomyces cerevisiae to improve glutathione production.Scientific reports · 2018Article
- Microbial production of glutathione.World journal of microbiology & biotechnology · 2017Review
- Article
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Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
backgroundL-glutathione (GSH) is a non-protein thiol compound with important biological properties and is widely used in pharmaceutical, food, cosmetic and health products. The cellular GSH is determined by the activity and characteristic of GSH-synthesizing enzymes, energy and precursor supply, and degradation of formed GSH.
resultsIn this study, genes encoding enzymes related to the precursor amino acid degradation and glycogen formation as well as GSH degradation were systematically manipulated in Escherichia coli strains over-expressing gshF from Actinobacillus succinogenes. The manipulation included disrupting the precursor degradation pathways (tnaA and sdaA), eliminating L-glutathione degradation (ggt and pepT), and manipulating the intracellular ATP level (disruption of glgB). However the constructed mutants showed lower levels of GshF expression. 2-D electrophoresis was performed to elucidate the reasons for this discrepancy, and the results indicated obvious changes in central metabolism and amino acid metabolism in the penta-mutant. Fed-batch culture of the penta-mutant ZJ12345 was performed where the GshF expression level was enhanced, and both the GSH production (19.10 mM) and the yield based on added L-cysteine (0.76 mmol/mmol) were significantly increased.
conclusionBy interrupting the degradation pathways of L-cysteine, serine and GSH and blocking glycogen formation, the GSH production efficiency was significantly improved.
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