Evidence map›Paper›PMID 37674094›Full record

ReviewNature protocols2023

Enzyme immobilization on covalent organic framework supports.

Qianqian Zhu, Yunlong Zheng, Zhenjie Zhang, Yao Chen

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 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Review
  2. RapidChemical science · 2026
    Article
  3. Nanomaterial Integration at Liquid-Liquid Interfaces for Green Catalysis.Advanced materials (Deerfield Beach, Fla.) · 2026
    Review
  4. Review
  5. Article
  6. Review
  7. Reticular Chemistry: A Versatile Platform for Engineering Heterogenous Biocatalysts.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Design, Synthesis, and Application of Immobilized Enzymes on Artificial Porous Materials.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

4 authors.

Qianqian Zhu *State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, P.R. China.
Yunlong Zheng *State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, P.R. China.
Zhenjie ZhangState Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, P.R. China. zhangzhenjie@nankai.edu.cn.ORCID 0000-0003-2053-3771
Yao ChenState Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, P.R. China. chenyao@nankai.edu.cn.ORCID 0000-0002-3465-7380

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymes are natural catalysts with high catalytic activity, substrate specificity and selectivity. Their widespread utilization in industrial applications is limited by their sensitivity to harsh reaction conditions and difficulties relating to their removal and re-use after the reaction is complete. These limitations can be addressed by immobilizing the enzymes in solid porous supports. Covalent organic frameworks (COFs) are ideal candidate carriers because of their good biocompatibility, long-term water stability and large surface area. In post-synthetic immobilization, the enzyme is added to an existing COF; this has had limited success because of enzyme leaching and pore blockage by enzymes that are too large. Direct-immobilization methods-building the COF around the enzyme-allow tailored incorporation of proteins of any size and result in materials with lower levels of leaching and better mass transport of reactants and products. This protocol describes direct-immobilization methods that can be used to fabricate enzyme@COF (@ = engulfing) biocomposites with rationally programmed structures and functions. If COF construction requires harsh reaction conditions, the enzyme can be protected by using a removable metal-organic framework. Alternatively, a direct in situ approach, in which the enzyme and the COF monomers assemble under very mild conditions, can be used. Examples of both approaches are described: enzyme@COF-42-B/43-B capsules (enzymes including catalase, glucose oxidase, etc.) with ZIF-90 or ZPF-2 as protectors, and lipase@NKCOF-98/99 via in situ direct-immobilization methods (synthesis timing: 30-100 min). Example assays for physical and functional characterization of the COF and enzyme@COF materials are also described.

Indexed as

Metal-Organic FrameworksBiological AssayCatalysisNanoparticlesPorosityMetal-Organic FrameworksZIF-90

Identifiers

What OpenQuestion 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 OpenQuestion graph.