Evidence map›Paper›PMID 42414308›Full record

ArticleNature communications2026

Mechanically locking enzymes in covalent organic frameworks via light-responsive nanohands for stable biocatalysis.

Tiantian Wang, Ruobing Xin, Yang Qian, Hongli Zhou, Jinlin Zhang, Qingshuang Yang, Peng Lei, Yongqi Pan, Haojie Geng, Hao Zhang and 2 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

12 authors.

Tiantian Wang *College of Chemistry and Chemical Engineering, Southwest University, Chongqing, China.
Ruobing Xin *State Key Laboratory of Chemical Engineering and Low-Carbon Technology, Department of Chemical Engineering, Tsinghua University, Beijing, China.
Yang Qian *College of Chemistry and Chemical Engineering, Southwest University, Chongqing, China.
Hongli Zhou *College of Chemistry and Chemical Engineering, Southwest University, Chongqing, China.
Jinlin Zhang *College of Chemistry and Chemical Engineering, Southwest University, Chongqing, China.
Qingshuang YangCollege of Chemistry and Chemical Engineering, Southwest University, Chongqing, China.
Peng LeiCollege of Chemistry and Chemical Engineering, Southwest University, Chongqing, China.
Yongqi PanState Key Laboratory of Chemical Engineering and Low-Carbon Technology, Department of Chemical Engineering, Tsinghua University, Beijing, China.
Haojie GengCollege of Chemistry and Chemical Engineering, Southwest University, Chongqing, China.ORCID http://orcid.org/0000-0003-0208-0190
Hao ZhangCollege of Chemistry and Chemical Engineering, Southwest University, Chongqing, China.
Yujun WangState Key Laboratory of Chemical Engineering and Low-Carbon Technology, Department of Chemical Engineering, Tsinghua University, Beijing, China.ORCID http://orcid.org/0000-0001-7782-3345
Qiang ChenCollege of Chemistry and Chemical Engineering, Southwest University, Chongqing, China. qiangchen@swu.edu.cn.ORCID http://orcid.org/0000-0001-9684-1098

Funding

Natural Science Foundation of Chongqing (Natural Science Foundation of Chongqing Municipality) CSTB2025NSCQ-GPX0483
6 · The paper itself

Abstract

Enzyme immobilization is pivotal to sustainable biocatalysis, yet the most widespread protocol of physical adsorption on static porous supports suffers from enzyme leakage and short catalytic lifespan. We introduce a dynamic-pore mechano-locking strategy employing tetrafluoroazobenzene-engineered covalent organic frameworks (COFs), where visible-light-mediated isomerization enables precise and reversible pore-size variation for adaptive enzyme confinement. This approach significantly enhances immobilization stability across diverse enzymes, improving the retention of horseradish peroxidase, cytochrome c, and laccase by 6.7-, 9.7-, and 1.8-fold, respectively. Mechanically locked formate dehydrogenase retained 99.2% activity after five cycles, surpassing most prior systems. In continuous-flow microreactors, productivity sustained over 22000 min, extending half-life 47-fold versus static-pore counterparts. Experimental and computational analyses reveal that synergistic pore compression and nanohands embedding during photoresponsive locking induce enzyme conformational restructuring and restricted residue mobility. This platform enables ultra-stable enzyme immobilization by orchestrating adaptive pore engineering with mechanically reinforced biocompatible interactions, unlocking broad potential for green biomanufacturing.

Indexed as

Enzymes, ImmobilizedMetal-Organic FrameworksBiocatalysisCytochromes cEnzyme StabilityFormate DehydrogenasesHorseradish PeroxidaseLaccaseLightPorosityCytochromes cEnzymes, ImmobilizedFormate DehydrogenasesHorseradish PeroxidaseLaccaseMetal-Organic Frameworks

Identifiers

PMID42414308
PMCPMC13473591

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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.