Evidence map›Paper›PMID 28253372›Full record

ArticlePloS one2017

Enhanced poly(3-hydroxypropionate) production via β-alanine pathway in recombinant Escherichia coli.

Stephen Tamekou Lacmata, Jules-Roger Kuiate, Yamei Ding, Mo Xian, Huizhou Liu, Thaddée Boudjeko, Xinjun Feng, Guang Zhao

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.6field-weighted citation impact, top 37% 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

6 citing papers in PubMed, 27 citations in OpenAlex.

  1. Article
  2. Advances in the synthesis of β-alanine.Frontiers in bioengineering and biotechnology · 2023
    Review
  3. Bio-conversion of organic wastes towards polyhydroxyalkanoates.Biotechnology notes (Amsterdam, Netherlands) · 2023
    Review
  4. Review
  5. Article
  6. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 2 countries.

Stephen Tamekou LacmataCAS Key Laboratory of Biobased Materials, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, China.
Jules-Roger KuiateLaboratory of Microbiology and Antimicrobials Substances, Department of Biochemistry, Faculty of Sciences, University of Dschang, Dschang, Cameroon.
Yamei DingInstitute of Oceanology, Chinese Academy of Sciences, Qingdao, China.
Mo XianCAS Key Laboratory of Biobased Materials, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, China.
Huizhou LiuCAS Key Laboratory of Biobased Materials, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, China.
Thaddée BoudjekoLaboratory of Phytoptotection and Valorization of Vegetals Resources, Biotechnology-Nkolbisson Center, Department of Biochemistry, University of Yaounde, Yaounde, Cameroon.
Xinjun FengCAS Key Laboratory of Biobased Materials, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, China.
Guang ZhaoCAS Key Laboratory of Biobased Materials, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, China.
Chinese Academy of Sciences · CNQingdao Institute of Bioenergy and Bioprocess Technology · CNUniversité de Dschang · CMUniversité de Yaoundé I · CM

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Poly(3-hydroxypropionate) (P3HP) is a thermoplastic with great compostability and biocompatibility, and can be produced through several biosynthetic pathways, in which the glycerol pathway achieved the highest P3HP production. However, exogenous supply of vitamin B12 was required to maintain the activity of glycerol dehydratase, resulting in high production cost. To avoid the addition of VB12, we have previously constructed a P3HP biosynthetic route with β-alanine as intermediate, and the present study aimed to improve the P3HP production of this pathway. L-aspartate decarboxylase PanD was found to be the rate-limiting enzyme in the β-alanine pathway firstly. To improve the pathway efficiency, PanD was screened from four different sources (Escherichia coli, Bacillus subtilis, Pseudomonas fluorescens, and Corynebacterium glutamicum). And PanD from C. glutamicum was found to have the highest activity, the P3HP production was improved in flask cultivation with this enzyme. To further improve the production, the host strain was screened and the culture condition was optimized. Under optimal conditions, production and content of P3HP reached to 10.2 g/L and 39.1% (wt/wt [cell dry weight]) in an aerobic fed-batch fermentation. To date, this is the highest P3HP production without VB12.

Indexed as

Recombination, Geneticbeta-AlanineCarboxy-LyasesElectrophoresis, Polyacrylamide GelEscherichia coliFermentationGenes, BacterialPlasmidsPolyestersaspartate 4-decarboxylasebeta-AlanineCarboxy-Lyasespoly(3-hydroxypropionate)Polyesters

Identifiers

PMID28253372
PMCPMC5333900
OpenAlexW2592225112

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.