Evidence map›Paper›PMID 37879963›Full record

ArticleFEBS open bio2023

Novel aminoacylases from Streptomyces griseus DSM 40236 and their recombinant production in Streptomyces lividans.

Gerrit Haeger, Johanna Probst, Karl-Erich Jaeger, Johannes Bongaerts, Petra Siegert

Open access · goldAbstract read
In one paragraph

Article in FEBS open bio, 2023. 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
0.7field-weighted citation impact, top 22% 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, 3 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

5 authors at 2 institutions in 1 country.

Gerrit HaegerInstitute of Nano- and Biotechnologies, Aachen University of Applied Sciences, Jülich, Germany.ORCID 0000-0001-5293-6992
Johanna ProbstInstitute of Nano- and Biotechnologies, Aachen University of Applied Sciences, Jülich, Germany.
Karl-Erich JaegerInstitute of Molecular Enzyme Technology, Heinrich Heine University Düsseldorf, Jülich, Germany.
Johannes BongaertsInstitute of Nano- and Biotechnologies, Aachen University of Applied Sciences, Jülich, Germany.ORCID 0009-0007-8656-1472
Petra SiegertInstitute of Nano- and Biotechnologies, Aachen University of Applied Sciences, Jülich, Germany.
FH Aachen · DEForschungszentrum Jülich · DE

Funding

Bundesministerium für Bildung und Forschung
6 · The paper itself

Abstract

Amino acid-based surfactants are valuable compounds for cosmetic formulations. The chemical synthesis of acyl amino acids is conventionally performed by the Schotten-Baumann reaction using fatty acyl chlorides, but aminoacylases have also been investigated for use in biocatalytic synthesis with free fatty acids. Aminoacylases and their properties are diverse; they belong to different peptidase families and show differences in substrate specificity and biocatalytic potential. Bacterial aminoacylases capable of synthesis have been isolated from Burkholderia, Mycolicibacterium, and Streptomyces. Although several proteases and peptidases from S. griseus have been described, no aminoacylases from this species have been identified yet. In this study, we investigated two novel enzymes produced by S. griseus DSM 40236

Indexed as

StreptomycesStreptomyces griseusAmidohydrolasesAmino AcidsHumansLysineStreptomyces lividansAmidohydrolasesAmino Acidsaminoacylase ILysineacyl amino acidsrecombinant expressionStreptomyces griseusStreptomyces lividansα-aminoacylaseε-lysine acylase

Identifiers

PMID37879963
PMCPMC10699109
OpenAlexW4387949990

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.