Evidence map›Paper›PMID 38204129›Full record

ArticleApplied microbiology and biotechnology2024

Novel recombinant aminoacylase from Paraburkholderia monticola capable of N-acyl-amino acid synthesis.

Gerrit Haeger, Tristan Jolmes, Sven Oyen, Karl-Erich Jaeger, Johannes Bongaerts, Ulrich Schörken, Petra Siegert

Open access · goldAbstract read
In one paragraph

Article in Applied microbiology and biotechnology, 2024. 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
2.3field-weighted citation impact, top 12% 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, 10 citations in OpenAlex.

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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

7 authors at 3 institutions in 1 country.

Gerrit HaegerInstitute of Nano- and Biotechnologies, Aachen University of Applied Sciences, 52428, Jülich, Germany.ORCID http://orcid.org/0000-0001-5293-6992
Tristan JolmesFaculty of Applied Natural Sciences, TH Köln University of Applied Sciences-Leverkusen Campus, Leverkusen, Germany.ORCID http://orcid.org/0000-0002-0963-0442
Sven OyenInstitute of Nano- and Biotechnologies, Aachen University of Applied Sciences, 52428, Jülich, Germany.
Karl-Erich JaegerInstitute of Molecular Enzyme Technology, Heinrich Heine University Düsseldorf, 52425, Jülich, Germany.ORCID http://orcid.org/0000-0002-6036-0708
Johannes BongaertsInstitute of Nano- and Biotechnologies, Aachen University of Applied Sciences, 52428, Jülich, Germany.ORCID http://orcid.org/0009-0007-8656-1472
Ulrich SchörkenFaculty of Applied Natural Sciences, TH Köln University of Applied Sciences-Leverkusen Campus, Leverkusen, Germany.ORCID http://orcid.org/0000-0003-3471-7651
Petra SiegertInstitute of Nano- and Biotechnologies, Aachen University of Applied Sciences, 52428, Jülich, Germany. siegert@fh-aachen.de.ORCID http://orcid.org/0000-0001-7172-3060
FH Aachen · DETH Köln - University of Applied Sciences · DEForschungszentrum Jülich · DE

Funding

Bundesministerium für Bildung und Forschung 13FH256PA6Bundesministerium für Bildung und Forschung 13FH256PB6
6 · The paper itself

Abstract

N-Acyl-amino acids can act as mild biobased surfactants, which are used, e.g., in baby shampoos. However, their chemical synthesis needs acyl chlorides and does not meet sustainability criteria. Thus, the identification of biocatalysts to develop greener synthesis routes is desirable. We describe a novel aminoacylase from Paraburkholderia monticola DSM 100849 (PmAcy) which was identified, cloned, and evaluated for its N-acyl-amino acid synthesis potential. Soluble protein was obtained by expression in lactose autoinduction medium and co-expression of molecular chaperones GroEL/S. Strep-tag affinity purification enriched the enzyme 16-fold and yielded 15 mg pure enzyme from 100 mL of culture. Biochemical characterization revealed that PmAcy possesses beneficial traits for industrial application like high temperature and pH-stability. A heat activation of PmAcy was observed upon incubation at temperatures up to 80 °C. Hydrolytic activity of PmAcy was detected with several N-acyl-amino acids as substrates and exhibited the highest conversion rate of 773 U/mg with N-lauroyl-L-alanine at 75 °C. The enzyme preferred long-chain acyl-amino-acids and displayed hardly any activity with acetyl-amino acids. PmAcy was also capable of N-acyl-amino acid synthesis with good conversion rates. The best synthesis results were obtained with the cationic L-amino acids L-arginine and L-lysine as well as with L-leucine and L-phenylalanine. Exemplarily, L-phenylalanine was acylated with fatty acids of chain lengths from C8 to C18 with conversion rates of up to 75%. N-lauroyl-L-phenylalanine was purified by precipitation, and the structure of the reaction product was verified by LC-MS and NMR. KEY POINTS: • A novel aminoacylase from Paraburkholderia monticola was cloned, expressed in E. coli and purified. • The enzyme PmAcy exhibits exceptional temperature and pH stability and a broad substrate spectrum. • Synthesis of acyl amino acids was achieved in good yields.

Indexed as

AmidohydrolasesAmino AcidsBurkholderiaceaeEscherichia coliHumansInfantPhenylalanineAmidohydrolasesAmino Acidsaminoacylase IPhenylalanineAcyl-amino acidsAcylationAminoacylaseBiocatalysisBiosurfactantsChaperone

Identifiers

PMID38204129
PMCPMC10781821
OpenAlexW4390697233

What OpenQuestion holds

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LicenceCC BY
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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.