Evidence map›Paper›PMID 40073133›Full record

ArticleScience advances2025

Enhanced activity and self-regeneration in dynameric cross-linked enzyme nanoaggregates.

Rui Wang, Shang Wang, Jinghua Chen, Yan Xu, Xiaowei Yu, Mihail Barboiu, Yan Zhang

Abstract read
In one paragraph

Article in Science advances, 2025. 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

7 authors.

Rui WangKey Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Life Sciences and Health Engineering, Jiangnan University, Wuxi, 214122, P.R. China.ORCID 0009-0006-4841-4263
Shang WangKey Laboratory of Industrial Biotechnology of Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, Jiangsu, 214122, P.R. China.ORCID 0000-0002-7006-7513
Jinghua ChenKey Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Life Sciences and Health Engineering, Jiangnan University, Wuxi, 214122, P.R. China.ORCID 0000-0001-8122-8450
Yan XuKey Laboratory of Industrial Biotechnology of Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, Jiangsu, 214122, P.R. China.
Xiaowei YuKey Laboratory of Industrial Biotechnology of Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, Jiangsu, 214122, P.R. China.ORCID 0000-0001-7967-6051
Mihail BarboiuAdaptive Supramolecular Nanosystems Group, Institut Européen des Membranes, University of Montpellier, CNRS UMR 5365, ENSCM, Place Eugène Bataillon, CC 047, F-34095 Montpellier, France.ORCID 0000-0003-0042-9483
Yan ZhangKey Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Life Sciences and Health Engineering, Jiangnan University, Wuxi, 214122, P.R. China.ORCID 0000-0003-2479-7555

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Directed evolution, enzyme design, and effective immobilization have been used to improve the catalytic activity. Dynamic polymers offer a promising platform to improve enzyme activity in aqueous solutions. Here, amphiphilic dynamers and lipase self-assemble into nanoparticles of 150- to 600-nanometer diameter, showing remarkable threefold enhancement in catalytic activity. In addition, they also demonstrated the ability to promote the reversible refolding of the partially or completely denatured lipase. The catalytic efficiency is completed with its more convenient handling of dynameric nanoparticles facilitating the efficient recovery and reuse of the enzyme with cost-effective uses. Molecular simulation studies revealed an in-depth understanding of how the dynamer action mechanism affects the conformational changes of lipase. The dynamer served as an effective hydrophobic support, facilitating the lid opening and substrate access to the catalytic triad, resulting in a substantial activation with an improved stability and recyclability of the lipase.

Indexed as

Enzymes, ImmobilizedLipaseNanoparticlesBiocatalysisEnzyme StabilityMolecular Dynamics SimulationEnzymes, ImmobilizedLipase

Identifiers

PMID40073133
PMCPMC11900872

What OpenQuestion holds

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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.