Evidence map›Paper›PMID 42680184›Full record

ArticleThe ISME journal2026

Bacterial family-VIII esterase displays dual activities: hydrolysis of polyester bioplastics and β-lactam antibiotics.

Harry Lerner, Diego Casaburi, Nele Charlott Meier, Léa Bernabeu, Marcel Eck, Stefan Mecking, David Schleheck

Abstract read
In one paragraph

Article in The ISME journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0cells of the map it votes in
0citing papers in PubMed
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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

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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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Harry LernerDepartment of Biology, University of Konstanz, 78457 Konstanz, Germany.ORCID 0000-0002-2004-6490
Diego CasaburiDepartment of Biology, University of Konstanz, 78457 Konstanz, Germany.
Nele Charlott MeierDepartment of Biology, University of Konstanz, 78457 Konstanz, Germany.
Léa BernabeuDepartment of Chemistry, University of Konstanz, 78457 Konstanz, Germany.
Marcel EckDepartment of Chemistry, University of Konstanz, 78457 Konstanz, Germany.
Stefan MeckingDepartment of Chemistry, University of Konstanz, 78457 Konstanz, Germany.
David SchleheckDepartment of Biology, University of Konstanz, 78457 Konstanz, Germany.ORCID 0000-0002-1327-4161

Funding

Carl-Zeiss FoundationUniversity of Konstanz
6 · The paper itself

Abstract

The plastisphere is a unique ecosystem with microbes colonizing and potentially degrading plastic debris in the environment, provided that the polymers are enzymatically accessible as substrates to drive microbial growth. It also harbors an unusually high occurrence of antibiotic resistance genes, suggesting plastic debris as a potential vector for antibiotic-resistant microorganisms. In this study, we investigated microbial communities in forest soil degrading an emerging type of bioplastics, aliphatic long-chain polyesters (LCAPs). Sequencing analysis revealed a family-VIII esterase strongly associated with LCAP depolymerization that showed high structural similarity to type C β-lactamases. Structural modeling and substrate docking analysis indicated catalytically favorable binding of both LCAP and β-lactam antibiotics. Furthermore, the active site appeared to be located in a large, wide-open groove, rather than in a tunnel, resulting in a protein with a striking "pac-man"-like structure. Heterologous expression and in vitro activity testing confirmed its dual functionality as plastic depolymerase and β-lactam hydrolase. Sequence analysis indicated the enzyme as membrane-associated lipoprotein likely to be directed to the outer membrane. The membrane anchoring of the enzyme may offer striking microbial-ecological benefits, by preventing enzyme loss especially in aqueous environments, by increased catalytic efficiency through high enzyme concentration at the cell-plastic interface, and by spatially linking catalysis with membrane transport, thereby limiting monomer loss to non-producing plastisphere-community members (cheaters). Hence, our study highlighted a plastic depolymerizing enzyme with a striking substrate spectrum, bridging plastics and antibiotics degradation, and provides intriguing perspectives for understanding the microbial physiology, ecology, and evolution of (bio)plastic degradation in the environment.

Indexed as

Bacteriabeta Lactam AntibioticsEsterasesPolyestersbeta-LactamasesHydrolysisModels, MolecularMolecular Docking SimulationPhylogenySequence Analysis, DNASoil Microbiologybeta Lactam Antibioticsbeta-LactamasesEsterasesPolyestersenzyme promiscuityfamily-VIII esteraselipoproteinplastic-degrading enzymespolyester biodegradationpolyester hydrolasesoil bacteriaβ-lactamase

Identifiers

PMID42680184
PMCPMC13533575

What OpenQuestion holds

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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.