Evidence map›Paper›PMID 34635076›Full record

ArticleBMC biotechnology2021

Reductive enzymatic dynamic kinetic resolution affording 115 g/L (S)-2-phenylpropanol.

Christian Rapp, Simone Pival-Marko, Erika Tassano, Bernd Nidetzky, Regina Kratzer

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in BMC biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

0 citing papers in PubMed, 7 citations in OpenAlex.

No citing paper in PubMed yet.

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

5 authors at 2 institutions in 1 country.

Christian RappInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, 8010, Graz, Austria.
Simone Pival-MarkoInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, 8010, Graz, Austria.
Erika TassanoDepartment of Chemistry, University of Graz, NAWI Graz, Heinrichstrasse 28, 8010, Graz, Austria.
Bernd NidetzkyInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, 8010, Graz, Austria.
Regina KratzerInstitute of Biotechnology and Biochemical Engineering, Graz University of Technology, NAWI Graz, 8010, Graz, Austria. regina.kratzer@tugraz.at.ORCID 0000-0002-9318-1247
Graz University of Technology · ATUniversity of Graz · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundPublished biocatalytic routes for accessing enantiopure 2-phenylpropanol using oxidoreductases afforded maximal product titers of only 80 mM. Enzyme deactivation was identified as the major limitation and was attributed to adduct formation of the aldehyde substrate with amino acid residues of the reductase.

resultsA single point mutant of Candida tenuis xylose reductase (CtXR D51A) with very high catalytic efficiency (43·10

conclusionThe current industrial production of profenols mainly relies on hydrolases. The bioreduction route established here represents an alternative method for the production of profenols that is competitive with hydrolase-catalyzed kinetic resolutions.

Indexed as

Aldehyde ReductaseCandidaKineticsPropanolsSubstrate Specificity1-phenylpropanolAldehyde ReductasePropanolsAldo–keto reductase engineeringBiocatalyst stabilityEnantiopure 2-aryl-1-propanolReductive dynamic kinetic resolution

Identifiers

PMID34635076
PMCPMC8507385
OpenAlexW3202460338

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.