Evidence map›Paper›PMID 40721475›Full record

ArticleScientific reports2025

Durable formulations of quorum quenching enzymes.

Reed Jacobson, Colton Castonguay, Mikael H Elias

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.

  1. Review
  2. Article
  3. 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

3 authors.

Reed Jacobson *Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, St. Paul, MN, 55108, USA.
Colton Castonguay *Biotechnology Institute, St. Paul, MN, 55108, USA.
Mikael H EliasDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, St. Paul, MN, 55108, USA. mhelias@umn.edu.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymes with industrial potential often face limitations due to stability and longevity constraints. Thermostable quorum quenching lactonases are appealing biotechnology tools for controlling microbial pathogenicity and biofilm formation via the interference of quorum sensing. However, the effective formulation of these enzymes remains a challenge. Here, we evaluate the resistance and activity of two thermostable quorum quenching lactonase enzymes (SsoPox and GcL) across diverse formulations relevant to industrial applications. We systematically tested these enzymes with 16 different crop adjuvants (including oils, an anti-foaming agent, surfactants, deposition aids, a water conditioner, and a sticking agent) over a 210-day period, demonstrating broad compatibility except with oil-based adjuvants. Additionally, both enzymes maintained their activity when incorporated into five different coating bases (acrylic, silicone, polyurethane, epoxy, and latex) with activity levels varying according to polymer type. Further investigation of enzymatic acrylic coating characterized the effects of salt water and temperature on enzyme activity levels. Functionalized coatings maintained remarkable stability over 250 days in both wet and dry conditions. These findings establish a practical demonstration and framework for integrating quorum quenching lactonases into industrial materials and formulations, significantly advancing their potential for 'real-world' applications for microbial control across multiple sectors.

Indexed as

Carboxylic Ester HydrolasesQuorum SensingEnzyme StabilityTemperatureCarboxylic Ester Hydrolases

Identifiers

PMID40721475
PMCPMC12304125

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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.