Evidence map›Paper›PMID 39441552›Full record

ArticleAngewandte Chemie (International ed. in English)2025

Targeted Genome Mining Facilitates the Discovery of a Promiscuous, Hyperthermostable Amidase from Thermovenabulum Gondwanense with Notable Nylon-Degrading Capacity.

Esther R Hoffman, Alana M M Rangaswamy, Maria E Cleveland, Jeffrey W Keillor, Graeme W Howe

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Microbial plastic degradation: enzymes, pathways, challenges, and perspectives.Microbiology and molecular biology reviews : MMBR · 2025
    Review
  8. Article
  9. Article
  10. An Update: Enzymatic Synthesis for Industrial Applications.Angewandte Chemie (International ed. in English) · 2025
    Review
  11. 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

5 authors.

Esther R HoffmanDepartment of Chemistry, Queen's University Chernoff Hall, 90 Bader Ln, Kingston, ON K7L 3N6, Canada.
Alana M M RangaswamyDepartment of Chemistry and Biomolecular Sciences, University of Ottawa, 10 Marie Curie Pvt, Ottawa, ON K1N 6N5, Canada.
Maria E ClevelandDepartment of Chemistry, Queen's University Chernoff Hall, 90 Bader Ln, Kingston, ON K7L 3N6, Canada.ORCID https://orcid.org/0000-0003-1923-0845
Jeffrey W KeillorDepartment of Chemistry and Biomolecular Sciences, University of Ottawa, 10 Marie Curie Pvt, Ottawa, ON K1N 6N5, Canada.
Graeme W HoweDepartment of Chemistry, Queen's University Chernoff Hall, 90 Bader Ln, Kingston, ON K7L 3N6, Canada.ORCID https://orcid.org/0000-0002-5976-0739

Funding

Natural Sciences and Engineering Research Council of Canada RGPIN-2019-05893Natural Sciences and Engineering Research Council of Canada RGPIN-2020-04455
6 · The paper itself

Abstract

Plastics are ubiquitous in our ecosystems, and microplastic accumulation in the environment is an emerging global health concern. Since available recycling technologies are not economically competitive with primary plastic production, global use is expected to reach 1231 megatons by 2060, with 493 megatons leeching into the environment each year. To identify new nylon-recycling biotechnologies, targeted genome mining was used to identify thermostable enzymes capable of degrading polyamides. Here, we describe the characterization of a novel protein sourced from Thermovenabulum gondwanense: TvgC. TvgC is extremely stable, exhibiting a melting temperature of 93 °C and no detectable losses in hydrolytic activity after one week at 60 °C. While nylonases primarily process nylon-6, TvgC catalysed the degradation of both nylon-6 and nylon-6,6 films, which are considerably more difficult to degrade. Finally, conversion experiments demonstrate that TvgC achieves a 1.2 wt % conversion of nylon-6 film, comparable to that of the most highly engineered nylonases. This novel hyperthermostable protein represents an excellent starting point for future engineering of increasingly efficient nylonases.

Indexed as

AmidohydrolasesNylonsCaprolactamPolymersamidaseAmidohydrolasesCaprolactamnylon 6NylonsPolymersbiocatalysisbioinformaticsNylCnylonaseplastic degradation

Identifiers

PMID39441552
PMCPMC11720373

What OpenQuestion holds

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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.