Evidence map›Paper›PMID 36235018›Full record

ArticleMolecules (Basel, Switzerland)2022

Simple Enzyme Immobilization for Flow Chemistry? An Assessment of Available Strategies for an Acetaldehyde-Dependent Aldolase.

Martin Wäscher, Thomas Classen, Jörg Pietruszka

Open access · goldAbstract read
In one paragraph

Article in Molecules (Basel, Switzerland), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 57% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. 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

3 authors at 2 institutions in 1 country.

Martin WäscherInstitute for Bioorganic Chemistry, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.ORCID 0000-0001-7001-7412
Thomas ClassenInstitute for Bio- and Geosciences 1: Bioorganic Chemistry, Forschungszentrum Jülich, 52425 Jülich, Germany.ORCID 0000-0002-3259-964X
Jörg PietruszkaInstitute for Bioorganic Chemistry, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.ORCID 0000-0002-9819-889X
Forschungszentrum Jülich · DEHeinrich Heine University Düsseldorf · DE

Funding

AiF "IGF-Vorhaben" 20341 BG
6 · The paper itself

Abstract

Enzyme immobilization is a technology that enables (bio-)catalysts to be applied in continuous-flow systems. However, there is a plethora of immobilization methods available with individual advantages and disadvantages. Here, we assessed the influence of simple and readily available methods with respect to the performance of 2-deoxy-d-ribose-5-phosphate aldolase (DERA) in continuous-flow conditions. The investigated immobilization strategies cover the unspecific attachment to carriers via epoxides, affinity-based attachment via metal ion affinity, StrepTag™-StrepTactin™ interaction as well as the covalent affinity attachment of an enzyme to a matrix tethered by the HaloTag

Indexed as

AcetaldehydeFructose-Bisphosphate AldolaseAldehyde-LyasesEnzymes, ImmobilizedEnzyme StabilityEpoxy CompoundsAcetaldehydeAldehyde-LyasesEnzymes, ImmobilizedEpoxy CompoundsFructose-Bisphosphate AldolasealdolaseDERAenzyme stabilityflow chemistryprocess optimization

Identifiers

PMID36235018
PMCPMC9570893
OpenAlexW4303954608

What OpenQuestion holds

Textmetadata
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.