Evidence map›Paper›PMID 39805935›Full record

ArticleScientific reports2025

Fine tuning enzyme activity assays for monitoring the enzymatic hydrolysis of PET.

Krisztina Boros, Blanka Eszter Nagy, Raluca Bianca Tomoiagă, Róbert Tőtős, Monica Ioana Toșa, Csaba Paizs, László Csaba Bencze

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 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.

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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.

Krisztina BorosEnzymology and Applied Biocatalysis Research Center, Faculty of Chemistry and Chemical Engineering, Babeș-Bolyai University, Arany János Street 11, 400028, Cluj-Napoca, Romania.
Blanka Eszter NagyEnzymology and Applied Biocatalysis Research Center, Faculty of Chemistry and Chemical Engineering, Babeș-Bolyai University, Arany János Street 11, 400028, Cluj-Napoca, Romania.
Raluca Bianca TomoiagăEnzymology and Applied Biocatalysis Research Center, Faculty of Chemistry and Chemical Engineering, Babeș-Bolyai University, Arany János Street 11, 400028, Cluj-Napoca, Romania.
Róbert TőtősEnzymology and Applied Biocatalysis Research Center, Faculty of Chemistry and Chemical Engineering, Babeș-Bolyai University, Arany János Street 11, 400028, Cluj-Napoca, Romania.
Monica Ioana ToșaEnzymology and Applied Biocatalysis Research Center, Faculty of Chemistry and Chemical Engineering, Babeș-Bolyai University, Arany János Street 11, 400028, Cluj-Napoca, Romania.
Csaba PaizsEnzymology and Applied Biocatalysis Research Center, Faculty of Chemistry and Chemical Engineering, Babeș-Bolyai University, Arany János Street 11, 400028, Cluj-Napoca, Romania.
László Csaba BenczeEnzymology and Applied Biocatalysis Research Center, Faculty of Chemistry and Chemical Engineering, Babeș-Bolyai University, Arany János Street 11, 400028, Cluj-Napoca, Romania. laszlo.bencze@ubbcluj.ro.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Efficient monitoring of the enzymatic PET-hydrolysis is crucial for developing novel plastic-degrading biocatalysts. Herein, we aimed to upgrade in terms of accuracy the analytical methods useful for monitoring enzymatic PET-degradation. For the HPLC-based assessment, the incorporation of an internal standard within the analytic procedure enabled a more accurate quantification of the overall TPA content and the assessment of molar distributions and relative content of each aromatic degradation product. The provided calibration curves cover a broad concentration range, from µM to low mM scale, facilitating assessment of both lower and higher PETase activities, with a limit of detection positioned below the reported PET-degrading activities. The increased reproducibility and accuracy of the improved HPLC method, compared to the previous methods, was supported by lower dispersion of product concentrations and their lower deviation from theoretical values over multiple measurements. The other predominantly employed UV-spectroscopy assay was also improved in terms of employed wavelength and medium extinction coefficient of the three aromatic degradation products, while being cross-validated by the improved HPLC method. Finally, both methods were used for monitoring the product formation within the leaf-branch compost cutinase (LCC)-mediated PET-hydrolysis and provided individual time-productivity profiles for each aromatic degradation product.

Indexed as

Carboxylic Ester HydrolasesEnzyme AssaysPolyethylene TerephthalatesChromatography, High Pressure LiquidHydrolysisReproducibility of ResultsCarboxylic Ester HydrolasescutinasePolyethylene Terephthalates

Identifiers

PMID39805935
PMCPMC11730307

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Registered trials

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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.