Evidence map›Paper›PMID 40302874›Full record

ArticleChem & bio engineering2025

Crystallization-Assisted Asymmetric Synthesis of Enantiopure Amines Using Membrane-Immobilized Transaminase.

Hippolyte Meersseman Arango, Neal Bachus, Xuan Dieu Linh Nguyen, Basile Bredun, Patricia Luis, Tom Leyssens, David Roura Padrosa, Francesca Paradisi, Damien P Debecker

Abstract read
In one paragraph

Article in Chem & bio engineering, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Engineering of ω-transaminases for advanced applications.Applied microbiology and biotechnology · 2026
    Review
  2. 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

9 authors.

Hippolyte Meersseman ArangoInstitute of Condensed Matter and Nanosciences (IMCN), Université Catholique de Louvain (UCLouvain), Place Louis Pasteur 1, 1348 Louvain-La-Neuve, Belgium.
Neal BachusInstitute of Condensed Matter and Nanosciences (IMCN), Université Catholique de Louvain (UCLouvain), Place Louis Pasteur 1, 1348 Louvain-La-Neuve, Belgium.
Xuan Dieu Linh NguyenInstitute of Condensed Matter and Nanosciences (IMCN), Université Catholique de Louvain (UCLouvain), Place Louis Pasteur 1, 1348 Louvain-La-Neuve, Belgium.
Basile BredunInstitute of Condensed Matter and Nanosciences (IMCN), Université Catholique de Louvain (UCLouvain), Place Louis Pasteur 1, 1348 Louvain-La-Neuve, Belgium.
Patricia LuisMaterials & Process Engineering (iMMC-IMAP), Université Catholique de Louvain, Place Sainte Barbe 2, 1348 Louvain-la-Neuve, Belgium.
Tom LeyssensInstitute of Condensed Matter and Nanosciences (IMCN), Université Catholique de Louvain (UCLouvain), Place Louis Pasteur 1, 1348 Louvain-La-Neuve, Belgium.ORCID https://orcid.org/0000-0001-7916-1373
David Roura PadrosaDepartment of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland.
Francesca ParadisiDepartment of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, 3012 Bern, Switzerland.ORCID https://orcid.org/0000-0003-1704-0642
Damien P DebeckerInstitute of Condensed Matter and Nanosciences (IMCN), Université Catholique de Louvain (UCLouvain), Place Louis Pasteur 1, 1348 Louvain-La-Neuve, Belgium.ORCID https://orcid.org/0000-0001-6500-2996

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The production of active pharmaceutical ingredients (APIs) requires enantiopure chiral amines, for which greener synthesis processes are needed. Transaminases (TAs) are enzymes that catalyze the enantioselective production of chiral amines from prochiral ketones through transamination under mild conditions. Yet, industrial applications of biocatalytic transamination remain currently hindered by the limited stability of soluble enzymes and by the unfavorable thermodynamic equilibrium of targeted asymmetric reactions. Enzyme immobilization can be applied to address stability, recoverability, and reusability issues. In the perspective of process intensification, we chose to immobilize TAs on polymeric (polypropylene) membranes. In the asymmetric synthesis of (R)-2-fluoro-α-methylbenzylamine ((R)-FMBA), such membrane-immobilized TAs exhibited superior specific activity and stability compared with soluble TAs; they also outperformed TAs immobilized on resins. The reaction yield remained, however, limited by thermodynamics. To further enhance the synthesis yield, the reaction was coupled with the

Identifiers

PMID40302874
PMCPMC12035565

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.