Evidence map›Paper›PMID 42186874›Full record

ArticleChembiochem : a European journal of chemical biology2026

Enhanced Enzyme Cascade Reactions Through Coencapsulation in Biocompatible Silica Nanoconfinement.

Ji-Soo Lee, Da-Hye Ryu, Myung Kyung Jung, Dong-Hyun You, So-Hee Park, Dae Youn Hwang, Beum-Soo An, Seung Yun Yang, Sungbaek Seo, Youngwoo Choi 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.

Ji-Soo LeeDepartment of Biomaterials Science, Pusan National University (PNU), Miryang-si, Republic of Korea.
Da-Hye RyuDepartment of Biomaterials Science, Pusan National University (PNU), Miryang-si, Republic of Korea.
Myung Kyung JungDepartment of Biomaterials Science, Pusan National University (PNU), Miryang-si, Republic of Korea.
Dong-Hyun YouDepartment of Biomaterials Science, Pusan National University (PNU), Miryang-si, Republic of Korea.
So-Hee ParkDepartment of Biomaterials Science, Pusan National University (PNU), Miryang-si, Republic of Korea.
Dae Youn HwangDepartment of Biomaterials Science, Pusan National University (PNU), Miryang-si, Republic of Korea.
Beum-Soo AnDepartment of Biomaterials Science, Pusan National University (PNU), Miryang-si, Republic of Korea.
Seung Yun YangDepartment of Biomaterials Science, Pusan National University (PNU), Miryang-si, Republic of Korea.
Sungbaek SeoDepartment of Biomaterials Science, Pusan National University (PNU), Miryang-si, Republic of Korea.
Youngwoo ChoiDepartment of Biomaterials Science, Pusan National University (PNU), Miryang-si, Republic of Korea.
Seong-Min JoDepartment of Biomaterials Science, Pusan National University (PNU), Miryang-si, Republic of Korea.ORCID https://orcid.org/0000-0001-9298-3793

Funding

Pusan National University
6 · The paper itself

Abstract

Enzyme cascade reactions, where the product of one enzyme serves as the substrate for another, are fundamental to cellular metabolism and essential for constructing efficient multi-enzyme systems. Spatial confinement of sequential enzymes can enhance cascade efficiency through proximity effects and substrate channeling, mimicking the organization of natural metabolic pathways. Here, we coencapsulated glucose oxidase (GOX) and horseradish peroxidase (HRP) within silica nanocapsules (SiNCs) using an enzyme-friendly synthesis method. The encapsulated enzymes retained high catalytic activity, and Michaelis-Menten kinetics analysis revealed decreased Km for GOX, indicating enhanced substrate affinity under confinement. The coencapsulated system demonstrated faster cascade kinetics compared to spatially separated enzyme configurations, providing direct evidence for the beneficial effects of enzyme proximity on intermediate transfer. Enhanced thermal stability of confined enzymes was also observed, presumably due to preserved hydration shells. This platform enables quantitative studies on enzyme behavior under nanoscale confinement, offering insights into the biochemical principles governing multi-enzyme cascade systems in both natural and artificial environments.

Indexed as

Biocompatible MaterialsGlucose OxidaseNanocapsulesSilicon DioxideBiocatalysisEnzymes, ImmobilizedHorseradish PeroxidaseKineticsBiocompatible MaterialsEnzymes, ImmobilizedGlucose OxidaseHorseradish PeroxidaseNanocapsulesSilicon Dioxideenzyme cascade reactionsenzyme confinementglucose oxidasehorseradish peroxidasesilica nanocapsules

Identifiers

PMID42186874
PMCPMC13206293

What OpenQuestion holds

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LicenceCC BY-NC
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.