Evidence map›Paper›PMID 27872998›Full record

ArticleApplied microbiology and biotechnology2017

PpEst is a novel PBAT degrading polyesterase identified by proteomic screening of Pseudomonas pseudoalcaligenes.

Paal W Wallace, Karolina Haernvall, Doris Ribitsch, Sabine Zitzenbacher, Matthias Schittmayer, Georg Steinkellner, Karl Gruber, Georg M Guebitz, Ruth Birner-Gruenberger

Abstract read
In one paragraph

Article in Applied microbiology and biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

  1. Article
  2. Paired genomic and proteomic analysis ofMicrobiology spectrum · 2026
    Article
  3. Article
  4. Disordered N-termini enhance the thermostability of SGNH-hydrolase family polyesterases.Protein science : a publication of the Protein Society · 2026
    Article
  5. Review
  6. Article
  7. Microbial plastic degradation: enzymes, pathways, challenges, and perspectives.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  8. Review
  9. Review
  10. Review
  11. Identification and Characterization of NewInternational journal of molecular sciences · 2025
    Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Review
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.

Paal W WallaceResearch Unit for Functional Proteomics and Metabolic Pathways, Institute of Pathology, Medical University of Graz, Stiftingtalstrasse 24, 8010, Graz, Austria.
Karolina HaernvallAustrian Centre of Industrial Biotechnology, Konrad Lorenz Strasse 20, 3430, Tulln, Austria.
Doris RibitschAustrian Centre of Industrial Biotechnology, Konrad Lorenz Strasse 20, 3430, Tulln, Austria.
Sabine ZitzenbacherAustrian Centre of Industrial Biotechnology, Petersgasse 14, 8010, Graz, Austria.
Matthias SchittmayerResearch Unit for Functional Proteomics and Metabolic Pathways, Institute of Pathology, Medical University of Graz, Stiftingtalstrasse 24, 8010, Graz, Austria.
Georg SteinkellnerAustrian Centre of Industrial Biotechnology, Petersgasse 14, 8010, Graz, Austria.
Karl GruberAustrian Centre of Industrial Biotechnology, Petersgasse 14, 8010, Graz, Austria.
Georg M GuebitzAustrian Centre of Industrial Biotechnology, Konrad Lorenz Strasse 20, 3430, Tulln, Austria.
Ruth Birner-GruenbergerResearch Unit for Functional Proteomics and Metabolic Pathways, Institute of Pathology, Medical University of Graz, Stiftingtalstrasse 24, 8010, Graz, Austria. ruth.birner-gruenberger@medunigraz.at.

Funding

Austrian Science Fund FWF W 1226
6 · The paper itself

Abstract

A novel esterase, PpEst, that hydrolyses the co-aromatic-aliphatic polyester poly(1,4-butylene adipate-co-terephthalate) (PBAT) was identified by proteomic screening of the Pseudomonas pseudoalcaligenes secretome. PpEst was induced by the presence of PBAT in the growth media and had predicted arylesterase (EC 3.1.1.2) activity. PpEst showed polyesterase activity on both whole and milled PBAT film releasing terephthalic acid and 4-(4-hydroxybutoxycarbonyl)benzoic acid while end product inhibition by 4-(4-hydroxybutoxycarbonyl)benzoic acid was observed. Modelling of an aromatic polyester mimicking oligomer into the PpEst active site indicated that the binding pocket could be big enough to accommodate large polymers. This is the first report of a PBAT degrading enzyme being identified by proteomic screening and shows that this approach can contribute to the discovery of new polymer hydrolysing enzymes. Moreover, these results indicate that arylesterases could be an interesting enzyme class for identifications of polyesterases.

Indexed as

Bacterial ProteinsBiodegradable PlasticsCarboxylic Ester HydrolasesCatalytic DomainGene ExpressionModels, MolecularPhthalic AcidsPolyestersProtein BindingProteomicsPseudomonas pseudoalcaligenesarylesteraseBacterial ProteinsBiodegradable PlasticsCarboxylic Ester HydrolasesPhthalic Acidspoly(butylene adipate-co-butylene terephthalate)Polyestersterephthalic acidArylesterasePoly(1,4-butylene adipate-co-terephthalate) (PBAT)PolyesterasePolymer degradationProteomicsSecretome

Identifiers

PMID27872998
PMCPMC5320007

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Registered trials

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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.