Evidence map›Paper›PMID 41427181›Full record

ArticleACS omega2025

Magnetically Recoverable δ‑FeOOH Particles for Multilayer Enzyme Immobilization and Surface-Induced Activity Tuning.

Francisco Lucas Chaves Almeida, Ederson Paulo Xavier Guilherme, Maria Isabel Rodriguez-Torres, Laura Rotilio, Magdalena Malankowska, Aliyeh Hasanzadeh, Bodil Fliis Holten, Suzana Siebenhaar, Lars Michael Skjolding, Jens P Morth and 3 more

Abstract read
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In one paragraph

Article in ACS omega, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

13 authors.

Francisco Lucas Chaves AlmeidaDepartment of Chemical and Biochemical Engineering, Technical University of Denmark, 2800 Kgs Lyngby, Denmark.ORCID https://orcid.org/0000-0001-5349-7645
Ederson Paulo Xavier GuilhermeBioprocess and Metabolic Engineering Laboratory, Department of Food Engineering and Technology, School of Food Engineering, University of Campinas, Rua Monteiro Lobato, 80CEP, Campinas, 13083-862 São Paulo, Brazil.
Maria Isabel Rodriguez-TorresDepartment of Chemical and Biochemical Engineering, Technical University of Denmark, 2800 Kgs Lyngby, Denmark.
Laura RotilioDepartment of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kgs Lyngby, Denmark.
Magdalena MalankowskaDepartment of Chemical and Biochemical Engineering, Technical University of Denmark, 2800 Kgs Lyngby, Denmark.
Aliyeh HasanzadehDepartment of Chemical and Biochemical Engineering, Technical University of Denmark, 2800 Kgs Lyngby, Denmark.
Bodil Fliis HoltenDepartment of Chemistry Organic and Inorganic Chemistry, Technical University of Denmark, 2800 Kgs Lyngby, Denmark.
Suzana SiebenhaarDepartment of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kgs Lyngby, Denmark.
Lars Michael SkjoldingDepartment of Environmental and Resource Engineering, Technical University of Denmark, 2800 Kgs Lyngby, Denmark.
Jens P MorthDepartment of Biotechnology and Biomedicine, Technical University of Denmark, 2800 Kgs Lyngby, Denmark.
John M WoodleyDepartment of Chemical and Biochemical Engineering, Technical University of Denmark, 2800 Kgs Lyngby, Denmark.ORCID https://orcid.org/0000-0002-7976-2483
Marcus Bruno Soares ForteBioprocess and Metabolic Engineering Laboratory, Department of Food Engineering and Technology, School of Food Engineering, University of Campinas, Rua Monteiro Lobato, 80CEP, Campinas, 13083-862 São Paulo, Brazil.ORCID https://orcid.org/0000-0002-2263-4392
Elif ErdemDepartment of Chemical and Biochemical Engineering, Technical University of Denmark, 2800 Kgs Lyngby, Denmark.ORCID https://orcid.org/0000-0003-1411-9793

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzyme immobilization is an effective strategy to enhance enzyme stability, which remains a major drawback in biocatalysis. However, achieving high enzyme loading without loss of activity is still a key limitation of conventional support. Most supports that overcome these limitations, such as nano- and microparticles, involve high production costs. Therefore, a support that combines the advantages of high surface area, easy recovery, and low-cost production is still lacking in the literature. In this study, we present a low-cost, dual-function, magnetically recoverable support material, superparamagnetic δ-FeOOH (feroxyhyte) particles, that enhances enzyme activity and modulates protein structure both prior to, and following immobilization. We show that δ-FeOOH enables lipase immobilization at loadings exceeding 60 mg g

Identifiers

PMID41427181
PMCPMC12713457

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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.