Evidence map›Paper›PMID 26586402›Full record

ArticleJournal of industrial microbiology & biotechnology2016

Glutathione production by recombinant Escherichia coli expressing bifunctional glutathione synthetase.

Dezheng Wang, Cheng Wang, Hui Wu, Zhimin Li, Qin Ye

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of industrial microbiology & biotechnology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Effects of acute iron overload on Nrf2-related glutathione metabolism in rat brain.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2021
    Article
  6. Article
  7. Article
  8. Review
  9. Microbial production of glutathione.World journal of microbiology & biotechnology · 2017
    Review
  10. Review
  11. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors.

Dezheng WangState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, 200237, Shanghai, China.
Cheng WangState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, 200237, Shanghai, China.
Hui WuState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, 200237, Shanghai, China. hwu@ecust.edu.cn.
Zhimin LiState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, 200237, Shanghai, China. lizm@ecust.edu.cn.
Qin YeState Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 130 Meilong Road, 200237, Shanghai, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glutathione (GSH) is an important bioactive substance applied widely in pharmaceutical and food industries. Due to the strong product inhibition in the GSH biosynthetic pathway, high levels of intracellular content, yield and productivity of GSH are difficult to achieve. Recently, a novel bifunctional GSH synthetase was identified to be less sensitive to GSH. A recombinant Escherichia coli strain expressing gshF encoding the bifunctional glutathione synthetase of Streptococcus thermophilus was constructed for GSH production. In this study, efficient GSH production using this engineered strain was investigated. The cultivation process was optimized by controlling dissolved oxygen (DO), amino acid addition and glucose feeding. 36.8 mM (11.3 g/L) GSH were formed at a productivity of 2.06 mM/h when the amino acid precursors (75 mM each) were added and glucose was supplied as the sole carbon and energy source.

Indexed as

Amino AcidsBiosynthetic PathwaysEnergy MetabolismEscherichia coliGlucoseGlutathioneGlutathione SynthaseMultifunctional EnzymesOxygenStreptococcus thermophilusAmino AcidsGlucoseGlutathioneGlutathione SynthaseMultifunctional EnzymesOxygenBifunctional glutathione synthetaseEnergy regenerationEscherichia coliGlutathioneOne-strain system

Identifiers

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.