Evidence map›Paper›PMID 42390021›Full record

ArticleChembiochem : a European journal of chemical biology2026

Reaction Optimization for Enzymatic Deconstruction of Industrially Relevant Nylon Composites.

Célestin Bourgery, Lance X Zhang, Dana L Carper, Muchu Zhou, Robert L Sacci, Matthew Korey, Lei Wang, Jessica H B Hemond, John F Cahill, Vera Bocharova and 1 more

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 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

11 authors.

Célestin BourgeryBiosciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA.ORCID https://orcid.org/0000-0002-7318-2218
Lance X ZhangBiosciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA.ORCID https://orcid.org/0000-0002-3381-9018
Dana L CarperBiosciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA.ORCID https://orcid.org/0000-0002-4758-8054
Muchu ZhouChemical Sciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA.ORCID https://orcid.org/0000-0001-8265-0215
Robert L SacciChemical Sciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA.ORCID https://orcid.org/0000-0002-0073-5221
Matthew KoreyManufacturing Sciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA.ORCID https://orcid.org/0000-0002-2285-5646
Lei WangTE Connectivity, Harrisburg, Pennsylvania, USA.
Jessica H B HemondTE Connectivity, Harrisburg, Pennsylvania, USA.
John F CahillBiosciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA.ORCID https://orcid.org/0000-0002-9866-4010
Vera BocharovaChemical Sciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA.ORCID https://orcid.org/0000-0003-4270-3866
Joshua K MichenerBiosciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee, USA.ORCID https://orcid.org/0000-0003-2302-8180

Funding

Advanced Materials and Manufacturing Technologies Office NFE-23-09933Basic Energy Sciences ERKCK55Oak Ridge National LaboratoryUT-Battelle, LLC DE-AC05-00OR22725Workforce Development for Teachers and Scientists
6 · The paper itself

Abstract

Plastics such as polyamides (PAs) possess unique physicochemical properties that make them indispensable in modern society. However, their energy-intensive production and challenging end-of-life management highlight the urgent need for efficient recycling or remanufacturing solutions. Enzymatic depolymerization offers a promising route toward circular recycling, yet remains constrained by limited enzyme characterization, lack of validation under industrially relevant conditions and substrates, and overall performance. Here, we optimized the reaction conditions for three recently discovered nylon-degrading enzymes. One of them, Nyl12, achieved product titers with PA6 and PA66 that exceed previously reported values, without enzyme engineering or substrate pretreatment. We further demonstrated the scalability of the process and its application to complex PA-based materials used in microelectronic components. Analysis of substrate features, including surface area and particle size, revealed key parameters governing enzymatic activity and provided a framework for future pretreatment and process optimization efforts. In combination, these efforts provide a new benchmark for enzymatic nylon recycling.

Indexed as

NylonsNylonsNylCnylonnylon hydrolasenylon recycling

Identifiers

PMID42390021
PMCPMC13325522

What OpenQuestion holds

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LicenceCC BY-NC-ND
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.