Evidence map›Paper›PMID 42252780›Full record

ArticleSmall (Weinheim an der Bergstrasse, Germany)2026

Enhanced Biocatalysis in Nanofluidic Membrane Reactors With Goldilocks Nanopores for Enzymes.

Wangsuk Oh, Ji-Woong Park

Abstract read
In one paragraph

Article in Small (Weinheim an der Bergstrasse, Germany), 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

2 authors.

Wangsuk OhSchool of Materials Science and Engineering, Gwangju Institute of Science and Technology, Gwangju, Republic of Korea.
Ji-Woong ParkSchool of Materials Science and Engineering, Gwangju Institute of Science and Technology, Gwangju, Republic of Korea.ORCID 0000-0002-8783-3675

Funding

Korea Basic Science InstituteNational Research Foundation 2021M3H4A3A02086779
6 · The paper itself

Abstract

Continuous-flow biocatalysis enables sustainable synthesis but suffers from diminished enzyme-substrate interactions under convective transport. Nanoconfinement addresses the challenge, yet the lack of tunable, flow-compatible nanoreactors has limited exploration of extreme confinement matching the enzyme dimension under flow. Here, we reveal an enzyme-scale confinement regime that maximizes enzymatic activity for flow reactions using enzyme-encapsulating molecular network membrane reactors with nanometer-scale pore tunability. Continuous-flow kinetic resolution identifies an optimal balance at an enzyme-to-average pore size ratio of ∼2, where confinement-enhanced substrate access within sub-minute space time is balanced against flow resistance. Under tight confinement, the apparent catalytic efficiency increases by up to 133-fold relative to free enzymes and achieves 30 000-fold higher specific space-time yield than conventional flow reactors. This work presents a tunable nanoreactor platform and establishes enzyme-scale confinement control as a key design principle for high-performance nanofluidic biocatalysis in flow-based synthesis and sensing.

Indexed as

BiocatalysisBioreactorsEnzymesMembranes, ArtificialNanoporesNanotechnologyContinuous Flow ChemistryKineticsEnzymesMembranes, Artificialbiocatalysisenzyme immobilizationflow chemistrymembrane nanoreactororganic sol‐gel synthesis

Identifiers

PMID42252780
PMCPMC13495852

What OpenQuestion holds

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LicenceCC BY-NC
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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.