Evidence map›Paper›PMID 25890272›Full record

ArticleMicrobial cell factories2015

Metabolic engineering of Escherichia coli for enhanced arginine biosynthesis.

Mireille Ginesy, Jaroslav Belotserkovsky, Josefine Enman, Leif Isaksson, Ulrika Rova

Open access · goldAbstract read
In one paragraph

Article in Microbial cell factories, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
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

23 citing papers in PubMed, 76 citations in OpenAlex.

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  11. TheMicroorganisms · 2022
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  14. Production of l-glutamate family amino acids inSynthetic and systems biotechnology · 2021
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  15. Article
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  17. Metabolic engineering ofEngineering in life sciences · 2019
    Article
  18. Article
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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 at 1 institution in 1 country.

Mireille GinesyBiochemical Process Engineering, Division of Chemical Engineering, Department of Civil, Environmental and Natural Resources Engineering, Luleå University of Technology, SE-971 87, Luleå, Sweden. mireille.ginesy@ltu.se.
Jaroslav BelotserkovskyDepartment of Molecular Biosciences Wenner-Gren institute, Stockholm University, SE-106 91, Stockholm, Sweden. jaroslav.belotserkovsky@su.se.
Josefine EnmanBiochemical Process Engineering, Division of Chemical Engineering, Department of Civil, Environmental and Natural Resources Engineering, Luleå University of Technology, SE-971 87, Luleå, Sweden. josefine.enman@ltu.se.
Leif IsakssonDepartment of Molecular Biosciences Wenner-Gren institute, Stockholm University, SE-106 91, Stockholm, Sweden. leif.isaksson@su.se.
Ulrika RovaBiochemical Process Engineering, Division of Chemical Engineering, Department of Civil, Environmental and Natural Resources Engineering, Luleå University of Technology, SE-971 87, Luleå, Sweden. ulrika.rova@ltu.se.
Luleå University of Technology · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundArginine is a high-value product, especially for the pharmaceutical industry. Growing demand for environmental-friendly and traceable products have stressed the need for microbial production of this amino acid. Therefore, the aim of this study was to improve arginine production in Escherichia coli by metabolic engineering and to establish a fermentation process in 1-L bioreactor scale to evaluate the different mutants.

resultsFirstly, argR (encoding an arginine responsive repressor protein), speC, speF (encoding ornithine decarboxylases) and adiA (encoding an arginine decarboxylase) were knocked out and the feedback-resistant argA214 or argA215 were introduced into the strain. Three glutamate independent mutants were assessed in bioreactors. Unlike the parent strain, which did not excrete any arginine during glucose fermentation, the constructs produced between 1.94 and 3.03 g/L arginine. Next, wild type argA was deleted and the gene copy number of argA214 was raised, resulting in a slight increase in arginine production (4.11 g/L) but causing most of the carbon flow to be redirected toward acetate. The V216A mutation in argP (transcriptional regulator of argO, which encodes for an arginine exporter) was identified as a potential candidate for improved arginine production. The combination of multicopy of argP216 or argO and argA214 led to nearly 2-fold and 3-fold increase in arginine production, respectively, and a reduction of acetate formation.

conclusionsIn this study, E. coli was successfully engineered for enhanced arginine production. The ∆adiA, ∆speC, ∆speF, ∆argR, ∆argA mutant with high gene copy number of argA214 and argO produced 11.64 g/L of arginine in batch fermentation, thereby demonstrating the potential of E. coli as an industrial producer of arginine.

Indexed as

Metabolic EngineeringArginineCarboxy-LyasesEscherichia coliEscherichia coli ProteinsGene Knockout TechniquesGlutamic AcidOrnithine DecarboxylasePlasmidsArgininearginine decarboxylaseCarboxy-LyasesEscherichia coli ProteinsGlutamic AcidOrnithine Decarboxylase

Identifiers

PMID25890272
PMCPMC4358701
OpenAlexW2121313480

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.