Evidence map›Paper›PMID 37006375›Full record

ArticleRSC advances2023

Mechanoenzymatic reactions for the hydrolysis of PET.

Esther Ambrose-Dempster, Leona Leipold, Dragana Dobrijevic, Maria Bawn, Eve M Carter, Gorjan Stojanovski, Tom D Sheppard, Jack W E Jeffries, John M Ward, Helen C Hailes

Full text read
In one paragraph

Article in RSC advances, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Lipases and Cutinases from Phytopathogenic and Saprobic Fungi in Plastic.Methods in molecular biology (Clifton, N.J.) · 2027
    Article
  2. Article
  3. Current advances in the structural biology and molecular engineering of PETase.Frontiers in bioengineering and biotechnology · 2023
    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

10 authors.

Esther Ambrose-DempsterDepartment of Chemistry, University College London 20 Gordon Street London WC1H 0AJ UK h.c.hailes@ucl.ac.uk.ORCID https://orcid.org/0000-0002-2954-2431
Leona LeipoldDepartment of Chemistry, University College London 20 Gordon Street London WC1H 0AJ UK h.c.hailes@ucl.ac.uk.ORCID https://orcid.org/0000-0002-7712-4293
Dragana DobrijevicDepartment of Biochemical Engineering, University College London Bernard Katz Building, Gower Street London WC1E 6BT UK.
Maria BawnDepartment of Biochemical Engineering, University College London Bernard Katz Building, Gower Street London WC1E 6BT UK.
Eve M CarterDepartment of Chemistry, University College London 20 Gordon Street London WC1H 0AJ UK h.c.hailes@ucl.ac.uk.ORCID https://orcid.org/0000-0002-0896-6884
Gorjan StojanovskiDepartment of Chemistry, University College London 20 Gordon Street London WC1H 0AJ UK h.c.hailes@ucl.ac.uk.ORCID https://orcid.org/0000-0003-4508-4124
Tom D SheppardDepartment of Chemistry, University College London 20 Gordon Street London WC1H 0AJ UK h.c.hailes@ucl.ac.uk.ORCID https://orcid.org/0000-0002-3455-1164
Jack W E JeffriesDepartment of Biochemical Engineering, University College London Bernard Katz Building, Gower Street London WC1E 6BT UK.
John M WardDepartment of Biochemical Engineering, University College London Bernard Katz Building, Gower Street London WC1E 6BT UK.ORCID https://orcid.org/0000-0002-4415-5544
Helen C HailesDepartment of Chemistry, University College London 20 Gordon Street London WC1H 0AJ UK h.c.hailes@ucl.ac.uk.ORCID https://orcid.org/0000-0001-5574-4742

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recent advances in the enzymatic degradation of poly(ethylene terphthalate) (PET) have led to a number of PET hydrolytic enzymes and mutants being developed. With the amount of PET building up in the natural world, there is a pressing need to develop scalable methods of breaking down the polymer into its monomers for recycling or other uses. Mechanoenzymatic reactions have gained traction recently as a green and efficient alternative to traditional biocatalytic reactions. For the first time we report increased yields of PET degradation by whole cell PETase enzymes by up to 27-fold by utilising ball milling cycles of reactive aging, when compared with typical solution-based reactions. This methodology leads to up to a 2600-fold decrease in the solvent required when compared with other leading degradation reactions in the field and a 30-fold decrease in comparison to reported industrial scale PET hydrolysis reactions.

Identifiers

PMID37006375
PMCPMC10050947

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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.