Evidence map›Paper›PMID 36336469›Full record

ArticleProtein science : a publication of the Protein Society2022

Investigation of the halophilic PET hydrolase PET6 from Vibrio gazogenes.

Sebastian Weigert, Pablo Perez-Garcia, Florian J Gisdon, Andreas Gagsteiger, Kristine Schweinshaut, G Matthias Ullmann, Jennifer Chow, Wolfgang R Streit, Birte Höcker

Open access · hybridAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 2 pooled it
1.5field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 2 syntheses or guidelines pooled it, 29 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. The effect of ionic strength on PETase enzymes: An experimental and computational study.Protein science : a publication of the Protein Society · 2026
    Article
  9. Article
  10. Article
  11. Review
  12. Review
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  15. Investigation of the halophilic PET hydrolase PET6 from Vibrio gazogenes.Protein science : a publication of the Protein Society · 2022
    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

9 authors at 2 institutions in 1 country.

Sebastian WeigertDepartment of Biochemistry, University of Bayreuth, Bayreuth, Germany.ORCID 0000-0002-0469-1545
Pablo Perez-GarciaDepartment of Microbiology and Biotechnology, University of Hamburg, Hamburg, Germany.ORCID 0000-0003-2248-3544
Florian J GisdonDepartment of Biochemistry, University of Bayreuth, Bayreuth, Germany.
Andreas GagsteigerDepartment of Biochemistry, University of Bayreuth, Bayreuth, Germany.ORCID 0000-0003-0112-3400
Kristine SchweinshautDepartment of Biochemistry, University of Bayreuth, Bayreuth, Germany.
G Matthias UllmannComputational Biochemistry, University of Bayreuth, Bayreuth, Germany.ORCID 0000-0002-6350-798X
Jennifer ChowDepartment of Microbiology and Biotechnology, University of Hamburg, Hamburg, Germany.ORCID 0000-0002-7499-5325
Wolfgang R StreitDepartment of Microbiology and Biotechnology, University of Hamburg, Hamburg, Germany.ORCID 0000-0001-7617-7396
Birte HöckerDepartment of Biochemistry, University of Bayreuth, Bayreuth, Germany.ORCID 0000-0002-8250-9462
University of Bayreuth · DEUniversität Hamburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The handling of plastic waste and the associated ubiquitous occurrence of microplastic poses one of the biggest challenges of our time. Recent investigations of plastic degrading enzymes have opened new prospects for biological microplastic decomposition as well as recycling applications. For polyethylene terephthalate, in particular, several natural and engineered enzymes are known to have such promising properties. From a previous study that identified new PETase candidates by homology search, we chose the candidate PET6 from the globally distributed, halophilic organism Vibrio gazogenes for further investigation. By mapping the occurrence of Vibrios containing PET6 homologs we demonstrated their ubiquitous prevalence in the pangenome of several Vibrio strains. The biochemical characterization of PET6 showed that PET6 has a comparatively lower activity than other enzymes but also revealed a superior turnover at very high salt concentrations. The crystal structure of PET6 provides structural insights into this adaptation to saline environments. By grafting only a few beneficial mutations from other PET degrading enzymes onto PET6, we increased the activity up to three-fold, demonstrating the evolutionary potential of the enzyme. MD simulations of the variant helped rationalize the mutational effects of those mutants and elucidate the interaction of the enzyme with a PET substrate. With tremendous amounts of plastic waste in the Ocean and the prevalence of Vibrio gazogenes in marine biofilms and estuarine marshes, our findings suggest that Vibrio and the PET6 enzyme are worthy subjects to study the PET degradation in marine environments.

Indexed as

HydrolasesVibrioHumansMicroplasticsPlasticsHydrolasesMicroplasticsPlasticshydrolasesMD simulationmetagenomePETasePET degradationpolyethylene terephthalatesubstrate interaction

Identifiers

PMID36336469
PMCPMC9679969
OpenAlexW4308299760

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.