Evidence map›Paper›PMID 37705789›Full record

ArticleNanoscale advances2023

Nanobiocatalysts with inbuilt cofactor recycling for oxidoreductase catalysis in organic solvents.

Jenny Sahlin, Congyu Wu, Andrea Buscemi, Claude Schärer, Seyed Amirabbas Nazemi, Rejaul S K, Nataly Herrera-Reinoza, Thomas A Jung, Patrick Shahgaldian

Abstract read
In one paragraph

Article in Nanoscale advances, 2023. 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. Review
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.

Jenny SahlinInstitute of Chemistry and Bioanalytics, School of Life Science, University of Applied Sciences and Arts Northwestern Switzerland Hofackerstrasse 30 Muttenz CH-4132 Switzerland patrick.shahgaldian@fhnw.ch.
Congyu WuInstitute of Chemistry and Bioanalytics, School of Life Science, University of Applied Sciences and Arts Northwestern Switzerland Hofackerstrasse 30 Muttenz CH-4132 Switzerland patrick.shahgaldian@fhnw.ch.
Andrea BuscemiInstitute of Chemistry and Bioanalytics, School of Life Science, University of Applied Sciences and Arts Northwestern Switzerland Hofackerstrasse 30 Muttenz CH-4132 Switzerland patrick.shahgaldian@fhnw.ch.
Claude SchärerInstitute of Chemistry and Bioanalytics, School of Life Science, University of Applied Sciences and Arts Northwestern Switzerland Hofackerstrasse 30 Muttenz CH-4132 Switzerland patrick.shahgaldian@fhnw.ch.
Seyed Amirabbas NazemiInstitute of Chemistry and Bioanalytics, School of Life Science, University of Applied Sciences and Arts Northwestern Switzerland Hofackerstrasse 30 Muttenz CH-4132 Switzerland patrick.shahgaldian@fhnw.ch.
Rejaul S KInstitute of Physics, University of Basel Klingelbergstrasse 82 Basel CH-4056 Switzerland.
Nataly Herrera-ReinozaLaboratory for X-ray Nanoscience and Technologies, Paul Scherrer Institute Forschungsstrasse 111 Villigen CH-5232 Switzerland.
Thomas A JungInstitute of Physics, University of Basel Klingelbergstrasse 82 Basel CH-4056 Switzerland.ORCID https://orcid.org/0000-0003-0717-9886
Patrick ShahgaldianInstitute of Chemistry and Bioanalytics, School of Life Science, University of Applied Sciences and Arts Northwestern Switzerland Hofackerstrasse 30 Muttenz CH-4132 Switzerland patrick.shahgaldian@fhnw.ch.ORCID https://orcid.org/0000-0002-1743-0387

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The major stumbling block in the implementation of oxidoreductase enzymes in continuous processes is their stark dependence on costly cofactors that are insoluble in organic solvents. We describe a chemical strategy that allows producing nanobiocatalysts, based on an oxidoreductase enzyme, that performs biocatalytic reactions in hydrophobic organic solvents without external cofactors. The chemical design relies on the use of a silica-based carrier nanoparticle, of which the porosity can be exploited to create an aqueous reservoir containing the cofactor. The nanoparticle core, possessing radial-centred pore channels, serves as a cofactor reservoir. It is further covered with a layer of reduced porosity. This layer serves as a support for the immobilisation of the selected enzyme yet allowing the diffusion of the cofactor from the nanoparticle core. The immobilised enzyme is, in turn, shielded by an organosilica layer of controlled thickness fully covering the enzyme. Such produced nanobiocatalysts are shown to catalyse the reduction of a series of relevant ketones into the corresponding secondary alcohols, also in a continuous flow fashion.

Identifiers

PMID37705789
PMCPMC10496889

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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.