Evidence map›Paper›PMID 41108613›Full record

ArticleAngewandte Chemie (International ed. in English)2025

Enzyme Immobilization in Porous Crystals via Cage Encapsulation.

Hong-Kun Liu, Takahiro Nakama, Shingo Funami, Risa Ebihara, Takaaki Mitsuhashi, Makoto Fujita

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Angewandte Chemie (International ed. in English), 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. Enzyme Immobilization in Porous Crystals via Cage Encapsulation.Angewandte Chemie (International ed. in English) · 2025
    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

6 authors.

Hong-Kun LiuDepartment of Applied Chemistry, School of Engineering, The University of Tokyo, Mitsui Link Lab Kashiwanoha 1, FS CREATION, 6-6-2 Kashiwanoha, Kashiwa, Chiba, 277-0882, Japan.
Takahiro NakamaDepartment of Applied Chemistry, School of Engineering, The University of Tokyo, Mitsui Link Lab Kashiwanoha 1, FS CREATION, 6-6-2 Kashiwanoha, Kashiwa, Chiba, 277-0882, Japan.ORCID 0000-0002-1023-7090
Shingo FunamiDepartment of Applied Chemistry, School of Engineering, The University of Tokyo, Mitsui Link Lab Kashiwanoha 1, FS CREATION, 6-6-2 Kashiwanoha, Kashiwa, Chiba, 277-0882, Japan.
Risa EbiharaDepartment of Applied Chemistry, School of Engineering, The University of Tokyo, Mitsui Link Lab Kashiwanoha 1, FS CREATION, 6-6-2 Kashiwanoha, Kashiwa, Chiba, 277-0882, Japan.ORCID 0000-0002-3499-6921
Takaaki MitsuhashiDepartment of Applied Chemistry, School of Engineering, The University of Tokyo, Mitsui Link Lab Kashiwanoha 1, FS CREATION, 6-6-2 Kashiwanoha, Kashiwa, Chiba, 277-0882, Japan.ORCID 0000-0001-7728-6869
Makoto FujitaTokyo College, U-Tokyo Institutes for Advanced Study (UTIAS), The University of Tokyo, Mitsui Link Lab Kashiwanoha 1, FS CREATION, 6-6-2 Kashiwanoha, Kashiwa, Chiba, 277-0882, Japan.ORCID 0000-0001-6105-7340

Funding

Aichi Science & Technology Foundation 2024P1002Iketani Science and Technology Foundation 0361165-AJapan Science Society 2024-2039Japan Synchrotron Radiation Research Institute 2022A1551Japan Synchrotron Radiation Research Institute 2022B1308Japan Synchrotron Radiation Research Institute 2023A1382Japan Synchrotron Radiation Research Institute 2023B1365Japan Synchrotron Radiation Research Institute 2024A1863Japan Synchrotron Radiation Research Institute 2024A2549Japan Synchrotron Radiation Research Institute 2024B1436JSPS Grants-in-Aid for Specially Promoted Research JP19H05461JSPS Grants-in-Aid for Specially Promoted Research JP21K14640JSPS Grants-in-Aid for Specially Promoted Research JP25K18122JSPS Research Fellowships for Young Scientists 23KJ0670JSPS Research Fellowships for Young Scientists 25KJ1156Photon Factory Program Advisory Committee 2023G604Photon Factory Program Advisory Committee 2024G001
6 · The paper itself

Abstract

Enzyme immobilization within solid or polymer matrices continues to face challenges, such as inhomogeneous protein environments, low loading efficiency, and limited versatility. Here, we present a pre-encapsulation strategy for enzyme immobilization in porous crystals via coordination cage encapsulation. In this approach, enzymes are first confined within the well-defined cavities of spherical coordination cages prior to crystallization. The host cage framework facilitates crystal formation under almost uniform conditions, independently of the surface properties of the enzymes. This isomorphous crystallization enabled the successful immobilization of nine proteins with diverse sizes and properties, achieving high loading efficiencies. The immobilized enzymes retained their native structures and catalytic activities within the crystal, functioning as heterogeneous catalysts with enhanced stability. Furthermore, the co-immobilization of two enzymes in close proximity facilitated cascade reactions, underscoring the potential of coordination cages as effective hosts for enzyme immobilization.

Indexed as

Enzymes, ImmobilizedCrystallizationPorosityEnzymes, ImmobilizedCage compoundsCrystal engineeringEnzyme catalysisHeterogeneous catalysisImmobilization

Identifiers

PMID41108613
PMCPMC12684350

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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.