Evidence map›Paper›PMID 28732539›Full record

ArticleJournal of nanobiotechnology2017

Enzyme adsorption-induced activity changes: a quantitative study on TiO

Augusto Márquez, Krisztina Kocsis, Gregor Zickler, Gilles R Bourret, Andrea Feinle, Nicola Hüsing, Martin Himly, Albert Duschl, Thomas Berger, Oliver Diwald

Abstract read
In one paragraph

Article in Journal of nanobiotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Production of Activated Carbons from Food/Storage Waste.Materials (Basel, Switzerland) · 2023
    Article
  2. Article
  3. Interactions of TiOChemical research in toxicology · 2020
    Article
  4. Particle Consolidation and Electron Transport in Anatase TiOACS applied materials & interfaces · 2019
    Article
  5. 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

10 authors.

Augusto MárquezDepartment of Chemistry and Physics of Materials, Paris Lodron University of Salzburg, Jakob-Haringer-Strasse 2a, 5020, Salzburg, Austria.
Krisztina KocsisDepartment of Chemistry and Physics of Materials, Paris Lodron University of Salzburg, Jakob-Haringer-Strasse 2a, 5020, Salzburg, Austria.
Gregor ZicklerDepartment of Chemistry and Physics of Materials, Paris Lodron University of Salzburg, Jakob-Haringer-Strasse 2a, 5020, Salzburg, Austria.
Gilles R BourretDepartment of Chemistry and Physics of Materials, Paris Lodron University of Salzburg, Jakob-Haringer-Strasse 2a, 5020, Salzburg, Austria.
Andrea FeinleDepartment of Chemistry and Physics of Materials, Paris Lodron University of Salzburg, Jakob-Haringer-Strasse 2a, 5020, Salzburg, Austria.
Nicola HüsingDepartment of Chemistry and Physics of Materials, Paris Lodron University of Salzburg, Jakob-Haringer-Strasse 2a, 5020, Salzburg, Austria.
Martin HimlyDepartment of Molecular Biology, Paris Lodron University of Salzburg, Hellbrunnerstrasse 34/III, 5020, Salzburg, Austria. Martin.Himly@sbg.ac.at.
Albert DuschlDepartment of Molecular Biology, Paris Lodron University of Salzburg, Hellbrunnerstrasse 34/III, 5020, Salzburg, Austria.
Thomas BergerDepartment of Chemistry and Physics of Materials, Paris Lodron University of Salzburg, Jakob-Haringer-Strasse 2a, 5020, Salzburg, Austria. Thomas.Berger@sbg.ac.at.ORCID http://orcid.org/0000-0002-2062-5193
Oliver DiwaldDepartment of Chemistry and Physics of Materials, Paris Lodron University of Salzburg, Jakob-Haringer-Strasse 2a, 5020, Salzburg, Austria.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundActivity retention upon enzyme adsorption on inorganic nanostructures depends on different system parameters such as structure and composition of the support, composition of the medium as well as enzyme loading. Qualitative and quantitative characterization work, which aims at an elucidation of the microscopic details governing enzymatic activity, requires well-defined model systems.

resultsVapor phase-grown and thermally processed anatase TiO

conclusionsThe study underlines that robust qualitative and quantitative statements about enzyme adsorption and activity retention require the use of model systems such as anatase TiO

Indexed as

Adsorptionbeta-GalactosidaseEnzyme ActivationHydrogen-Ion ConcentrationMicroscopy, Electron, ScanningNanoparticlesParticle SizePorositySurface PropertiesTitaniumWaterbeta-GalactosidaseTitaniumtitanium dioxideWaterAdsorptionAgglomeratesEnzymatic activityIR spectroscopyNanoparticlesTiO2β-galactosidase

Identifiers

PMID28732539
PMCPMC5521066

What OpenQuestion holds

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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.