Evidence map›Paper›PMID 37198321›Full record

ReviewNature protocols2023

Encapsulating and stabilizing enzymes using hydrogen-bonded organic frameworks.

Guosheng Chen, Siming Huang, Xiaomin Ma, Rongwei He, Gangfeng Ouyang

Abstract readReview
PubMed Publisher
In one paragraph

Review in Nature protocols, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
10.7field-weighted citation impact, top 1% of its field
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

22 citing papers in PubMed, 107 citations in OpenAlex.

  1. Article
  2. Article
  3. A Cholesterol Analogue for Cell-Surface Enzyme Display.Angewandte Chemie (International ed. in English) · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Reticular Chemistry: A Versatile Platform for Engineering Heterogenous Biocatalysts.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  8. Article
  9. Enzyme Immobilization in Porous Crystals via Cage Encapsulation.Angewandte Chemie (International ed. in English) · 2025
    Article
  10. Article
  11. Article
  12. Design, Synthesis, and Application of Immobilized Enzymes on Artificial Porous Materials.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
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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

5 authors at 3 institutions in 1 country.

Guosheng ChenMOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen University, Guangzhou, China. chengsh39@mail.sysu.edu.cn.ORCID 0000-0002-6540-7675
Siming HuangSchool of Pharmaceutical Sciences, Guangzhou Medical University, Guangzhou, China.
Xiaomin MaCryo-EM Center, Southern University of Science and Technology, Shenzhen, China.
Rongwei HeSchool of Chemical Engineering and Technology, Sun Yat-sen University, Zhuhai, China.
Gangfeng OuyangMOE Key Laboratory of Bioinorganic and Synthetic Chemistry, School of Chemistry, Sun Yat-sen University, Guangzhou, China. cesoygf@mail.sysu.edu.cn.ORCID 0000-0002-0797-6036
Sun Yat-sen University · CNGuangzhou Medical University · CNSouthern University of Science and Technology · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymes are outstanding natural catalysts with exquisite 3D structures, initiating countless life-sustaining biotransformations in living systems. The flexible structure of an enzyme, however, is highly susceptible to non-physiological environments, which greatly limits its large-scale industrial applications. Seeking suitable supports to immobilize fragile enzymes is one of the most efficient routes to ameliorate the stability problem. This protocol imparts a new bottom-up strategy for enzyme encapsulation using a hydrogen-bonded organic framework (HOF-101). In short, the surface residues of the enzyme can trigger the nucleation of HOF-101 around its surface through the hydrogen-bonded biointerface. As a result, a series of enzymes with different surface chemistries are able to be encapsulated within a highly crystalline HOF-101 scaffold, which has long-range ordered mesochannels. The details of experimental procedures are described in this protocol, which involve the encapsulating method, characterizations of materials and biocatalytic performance tests. Compared with other immobilization methods, this enzyme-triggering HOF-101 encapsulation is easy to operate and affords higher loading efficiency. The formed HOF-101 scaffold has an unambiguous structure and well-arranged mesochannels, favoring mass transfer and understanding of the biocatalytic process. It takes ~13.5 h for successful synthesis of enzyme-encapsulated HOF-101, 3-4 d for characterizations of materials and ~4 h for the biocatalytic performance tests. In addition, no specific expertise is necessary for the preparation of this biocomposite, although the high-resolution imaging requires a low-electron-dose microscope technology. This protocol can provide a useful methodology to efficiently encapsulate enzymes and design biocatalytic HOF materials.

Indexed as

ElectronsHydrogenResearch DesignHydrogen

Identifiers

PMID37198321
OpenAlexW4376873200

What Socratic holds

Textmetadata
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 Socratic graph.