Evidence map›Paper›PMID 39918853›Full record

ArticleChemPlusChem2025

Sustainable One-Pot Electrochemical Approach for Entrapment of Multi-Enzymes and Biocompatible Redox Mediator.

Hathaichanok Seelajaroen, Felix Mayr, Dominik Wielend, Munise Cobet, Christoph Ulbricht, Niyazi Serdar Sariciftci, Serpil Tekoglu

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in ChemPlusChem, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

7 authors.

Hathaichanok SeelajaroenLinz Institute for Organic Solar Cells (LIOS), Institute of Physical Chemistry, Johannes Kepler University Linz, Altenberger Str 69, A-4040, Linz, Austria.
Felix MayrLinz Institute for Organic Solar Cells (LIOS), Institute of Physical Chemistry, Johannes Kepler University Linz, Altenberger Str 69, A-4040, Linz, Austria.
Dominik WielendLinz Institute for Organic Solar Cells (LIOS), Institute of Physical Chemistry, Johannes Kepler University Linz, Altenberger Str 69, A-4040, Linz, Austria.
Munise CobetLinz Institute for Organic Solar Cells (LIOS), Institute of Physical Chemistry, Johannes Kepler University Linz, Altenberger Str 69, A-4040, Linz, Austria.
Christoph UlbrichtLinz Institute for Organic Solar Cells (LIOS), Institute of Physical Chemistry, Johannes Kepler University Linz, Altenberger Str 69, A-4040, Linz, Austria.
Niyazi Serdar SariciftciLinz Institute for Organic Solar Cells (LIOS), Institute of Physical Chemistry, Johannes Kepler University Linz, Altenberger Str 69, A-4040, Linz, Austria.
Serpil TekogluLinz Institute for Organic Solar Cells (LIOS), Institute of Physical Chemistry, Johannes Kepler University Linz, Altenberger Str 69, A-4040, Linz, Austria.ORCID 0000-0003-4352-7972

Funding

Austrian Science Foundation (FWF) Z222N19European Regional Development Fund (EFRE) GZ2018-98279-2Linz Institute of Technology (JKU Linz) LIT-2022-11-YOU-221
6 · The paper itself

Abstract

Enzyme immobilization is regarded as a key factor for their effective utilization in various fields such as biofuel production, wastewater treatment, and biosensors. Designing new electrodes with biocompatible support matrices is essential to improve the stability in bioelectrocatalysis. Modified carbon felt electrodes were prepared and tested as bioelectrocatalyst under mild conditions - aqueous media at room temperature and basically neutral pH. Co-immobilization of dehydrogenase enzymes and neutral red (NR) dye at carbon felt electrodes was successfully achieved during electropolymerization of pyrrole in a facile one-step approach. Neutral red was incorporated to operate as a redox mediator supporting efficient electron transfer to the enzymes' active sites. Electrodes modified with alcohol dehydrogenase (ADH) have been employed to reduce acetaldehyde to ethanol in a chronoamperometic setting with Faradaic efficiency (FE) of up to 33 %. By incorporating the cascade reaction with three enzymes - ADH, formate dehydrogenase, and formaldehyde dehydrogenase - an electroreduction sequence could be established to produce methanol from CO

Indexed as

Alcohol DehydrogenaseAldehyde OxidoreductasesBiocompatible MaterialsElectrochemical TechniquesEnzymes, ImmobilizedFormate DehydrogenasesElectrodesOxidation-ReductionAlcohol DehydrogenaseAldehyde OxidoreductasesBiocompatible MaterialsEnzymes, ImmobilizedFormate DehydrogenasesBioelectrocatalysisCO2 reductionDehydrogenasesEnzyme immobilizationNeutral redPolyypyrrole

Identifiers

PMID39918853
PMCPMC12105433

What OpenQuestion holds

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LicenceCC BY
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.