Evidence map›Paper›PMID 40781260›Full record

ArticleScientific reports2025

Carnivorous plants can decompose the polyesters poly(ethylene terephthalate) and poly(butylene adipate terephthalate).

Chiara Siracusa, Sebastian Gritsch, Robert Vielnascher, Moritz Dielacher, Milica Krunic, Felice Quartinello, Georg M Guebitz

Abstract read
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

7 authors.

Chiara Siracusaacib GmbH, Konrad-Lorenz-Strasse 20, Tulln an der Donau, 3430, Austria.ORCID http://orcid.org/0000-0003-0429-9946
Sebastian GritschInstitute of Environmental Biotechnology, Department of Agricultural Sciences, BOKU University, Konrad-Lorenz-Strasse 20, Tulln an der Donau, 3430, Austria.ORCID http://orcid.org/0000-0002-7509-4289
Robert VielnascherInstitute of Environmental Biotechnology, Department of Agricultural Sciences, BOKU University, Konrad-Lorenz-Strasse 20, Tulln an der Donau, 3430, Austria.ORCID http://orcid.org/0000-0002-5160-8070
Moritz DielacherInstitute of Environmental Biotechnology, Department of Agricultural Sciences, BOKU University, Konrad-Lorenz-Strasse 20, Tulln an der Donau, 3430, Austria.ORCID http://orcid.org/0009-0006-1985-4112
Milica KrunicDepartment of Bio Data Science, Faculty of Engineering, University of Applied Sciences Wiener Neustadt, Tulln an der Donau, Austria.ORCID http://orcid.org/0000-0001-5529-354X
Felice Quartinelloacib GmbH, Konrad-Lorenz-Strasse 20, Tulln an der Donau, 3430, Austria. felice.quartinello@boku.ac.at.ORCID http://orcid.org/0000-0001-9014-1621
Georg M Guebitzacib GmbH, Konrad-Lorenz-Strasse 20, Tulln an der Donau, 3430, Austria.ORCID http://orcid.org/0000-0003-2262-487X

Funding

European Union's Horizon2020- project UPLIFT 953073
6 · The paper itself

Abstract

Plants from the Nepenthes genus, which enumerates approximately 120 species, possess specialized pitchers enabling them to capture and digest various preys, mainly arthropods, from which the plants derive nutrients. The pitcher fluid contains many molecules of noteworthy importance, including antimicrobial compounds, traditionally used in medicine, as well as hydrolytic enzymes for prey digestion. In this study, polyesters films made from poly(ethylene terephthalate) (PET) and from poly(butylene adipate -co- terephthalate) (PBAT) were incubated in the pitcher of the carnivorous plants Nepenthes alata and Sarracenia purpurea. High performance liquid chromatography analysis revealed hydrolysis into their corresponding monomers, while hydrolysis efficiency was up to ten times higher in the presence of dried mealworm Tenebrio molitor and jasmonic acid. Proteomic analysis indicated the presence of the aspartic proteinase nepenthesin in most conditions, with high abundance in 70% of polyester-containing conditions compared to those without polyesters. Molecular docking simulations further suggested that nepenthesin has the potential to hydrolyze polyesters. While in contrast to cutinases there is only little information on hydrolysis of PET and PBAT by proteases in the literature, this work clearly demonstrates hydrolysis of both PET and PBAT by the recombinant protease nepenthesin, releasing similar amounts of TPA as the cutinase from Humicola insolens. These results suggest carnivorous plant fluids as a source for new enzymes for industrial applications such as for polyester hydrolysis.

Indexed as

PolyestersPolyethylene TerephthalatesAnimalsHydrolysisMolecular Docking Simulationpoly(butylene adipate-co-butylene terephthalate)PolyestersPolyethylene TerephthalatesCarnivorous plantsEnzymatic hydrolysisNepenthesinProteomic

Identifiers

PMID40781260
PMCPMC12334762

What OpenQuestion holds

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LicenceCC BY-NC-ND
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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.