Evidence map›Paper›PMID 35518281›Full record

ArticleRSC advances2020

A two-enzyme cascade reaction consisting of two reaction pathways. Studies in bulk solution for understanding the performance of a flow-through device with immobilised enzymes.

Nicolas Ghéczy, Kai Sasaki, Makoto Yoshimoto, Sajad Pour-Esmaeil, Martin Kröger, Pasquale Stano, Peter Walde

Open access · goldAbstract read
In one paragraph

Article in RSC advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

7 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Biocatalysis in Continuous-Flow Microfluidic Reactors.Advances in biochemical engineering/biotechnology · 2022
    Article
  5. Article
  6. 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

7 authors at 3 institutions in 3 countries.

Nicolas GhéczyLaboratory for Multifunctional Materials, Department of Materials, ETH Zürich Vladimir-Prelog-Weg 5 CH-8093 Zürich Switzerland peter.walde@mat.ethz.ch.ORCID https://orcid.org/0000-0002-7716-4893
Kai SasakiLaboratory for Multifunctional Materials, Department of Materials, ETH Zürich Vladimir-Prelog-Weg 5 CH-8093 Zürich Switzerland peter.walde@mat.ethz.ch.ORCID https://orcid.org/0000-0003-4865-8760
Makoto YoshimotoLaboratory for Multifunctional Materials, Department of Materials, ETH Zürich Vladimir-Prelog-Weg 5 CH-8093 Zürich Switzerland peter.walde@mat.ethz.ch.ORCID https://orcid.org/0000-0001-7489-229X
Sajad Pour-EsmaeilLaboratory for Multifunctional Materials, Department of Materials, ETH Zürich Vladimir-Prelog-Weg 5 CH-8093 Zürich Switzerland peter.walde@mat.ethz.ch.ORCID https://orcid.org/0000-0002-6637-8212
Martin KrögerPolymer Physics, Department of Materials, ETH Zürich Leopold-Ruzicka-Weg 4 CH-8093 Zürich Switzerland.ORCID https://orcid.org/0000-0003-1402-6714
Pasquale StanoDepartment of Biological and Environmental Sciences and Technologies (DiSTeBA), University of Salento Ecotekne 73100 Lecce Italy.ORCID https://orcid.org/0000-0002-2228-2825
Peter WaldeLaboratory for Multifunctional Materials, Department of Materials, ETH Zürich Vladimir-Prelog-Weg 5 CH-8093 Zürich Switzerland peter.walde@mat.ethz.ch.ORCID https://orcid.org/0000-0002-0827-0545
ETH Zurich · CHUniversity of Salento · ITYamaguchi University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzyme-catalysed cascade reactions in flow-through systems with immobilised enzymes currently are of great interest for exploring their potential for biosynthetic and bioanalytical applications. Basic studies in this field often aim at understanding the stability of the immobilised enzymes and their catalytic performance, for example, in terms of yield of a desired reaction product, analyte detection limit, enzyme stability or reaction reproducibility. In the work presented, a cascade reaction involving the two enzymes bovine carbonic anhydrase (BCA) and horseradish peroxidase (HRP) - with hydrogen peroxide (H

Identifiers

PMID35518281
PMCPMC9053938
OpenAlexW3024471569

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.