Evidence map›Paper›PMID 41221540›Full record

ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026

A Modular Biosensor Platform for the Detection of Plastic Monomers and the Engineering of Promiscuous Amidases Toward Challenging Substrates.

Ina Somvilla, Hannah Meier, Florian Oehlschläger, Hannes Meinert, Lena Koch, Patrick Ihrle, Katharina M Mehnert, Morten Flieger, Jonas Boß, Marco Seifert and 3 more

Abstract read
In one paragraph

Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

13 authors.

Ina SomvillaDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.ORCID https://orcid.org/0009-0000-7790-0566
Hannah MeierDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.ORCID https://orcid.org/0009-0009-3696-4059
Florian OehlschlägerDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.ORCID https://orcid.org/0009-0007-7416-0903
Hannes MeinertDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.ORCID https://orcid.org/0000-0001-6545-5047
Lena KochDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.ORCID https://orcid.org/0009-0004-1326-4416
Patrick IhrleDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.
Katharina M MehnertDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.ORCID https://orcid.org/0009-0003-9925-2071
Morten FliegerDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.ORCID https://orcid.org/0009-0001-0923-7026
Jonas BoßDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.
Marco SeifertDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.
Dominique BöttcherDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.ORCID https://orcid.org/0000-0001-9981-014X
Uwe T BornscheuerDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.ORCID https://orcid.org/0000-0003-0685-2696
Thomas BayerDepartment of Biotechnology & Enzyme Catalysis, Institute of Biochemistry, University of Greifswald, Felix-Hausdorff-Str. 4, 17487, Greifswald, Germany.ORCID https://orcid.org/0000-0002-0656-3280

Funding

Austrian Science Fund J4231-B21
6 · The paper itself

Abstract

Stable chemical bonds dictate the properties of industrial chemicals and materials. Particularly the persistence of synthetic polymers like polyurethanes (PUs) contributes to the global issues of waste accumulation and environmental pollution. To accelerate the discovery and engineering of plastic-degrading biocatalysts, a genetically encoded biosensor platform is established that enzymatically converts polyfunctionalized monomers into (aliphatic) aldehydes and allows their robust detection by a bacterial luciferase. In vivo, in vitro, and hybrid applications of the investigated biosensor system facilitate the bioluminescence-based assessment of the promiscuous esterase, amidase, and urethanase activity of amidase signature family enzymes, circumventing chromatographic analysis. Furthermore, the biosensor platform guides the selection of improved variants in a site-saturated enzyme library, exhibiting up to 5.5-fold enhanced activity toward difficult to hydrolyze screening molecules, including N-substituted decanamides, a representative polyether dicarbamate, and a commercial polyester-PU. The latter contain polyols like diethylene glycol, for which biosensor applications are scarce. Hence, this biosensor platform is not only the first to enable the monitoring of amidase and urethanase activity independent of chromogenic/fluorogenic molecules in real-time. It expands the detection scope of bacterial luciferases toward plastic monomers like polyols, which will aid advancing current recycling strategies for PU waste and beyond.

Indexed as

AmidohydrolasesBiosensing TechniquesPlasticsPolyurethanesAmidohydrolasesPlasticsPolyurethanesgenetically encoded biosensorhigh‐throughput screeningluciferaseplastic degradationurethanase engineering

Identifiers

PMID41221540
PMCPMC12866861

What OpenQuestion holds

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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.