Evidence map›Paper›PMID 39453420›Full record

ReviewApplied microbiology and biotechnology2024

Perspectives of aminoacylases in biocatalytic synthesis of N-acyl-amino acids surfactants.

Gerrit Haeger, Jessika Wirges, Johannes Bongaerts, Ulrich Schörken, Petra Siegert

Abstract readReview
In one paragraph

Review 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 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. International journal of systematic and evolutionary microbiology · 2025
    Article
  4. 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.

Gerrit HaegerNovo Nordisk, Novo Nordisk Park 1, 2760, Måløv, Denmark.ORCID http://orcid.org/0000-0001-5293-6992
Jessika WirgesInstitute of Nano- and Biotechnologies, Aachen University of Applied Sciences, Heinrich-Mussmannstr. 1, 52428, Jülich, Germany.
Johannes BongaertsInstitute of Nano- and Biotechnologies, Aachen University of Applied Sciences, Heinrich-Mussmannstr. 1, 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, 51379, Leverkusen, Germany.ORCID http://orcid.org/0000-0003-3471-7651
Petra SiegertInstitute of Nano- and Biotechnologies, Aachen University of Applied Sciences, Heinrich-Mussmannstr. 1, 52428, Jülich, Germany. siegert@fh-aachen.de.ORCID http://orcid.org/0000-0001-7172-3060

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many industrial processes are performed using harmful chemicals. The current technical synthesis of N-acyl-amino acids relies on acyl chlorides, which are typically obtained from phosgene chemistry. A greener alternative is the application of whole cells or enzymes to carry out synthesis in an environmentally friendly manner. Aminoacylases belong to the hydrolase family and the resolution of racemic mixtures of N-acetyl-amino acids is a well-known industrial process. Several new enzymes accepting long-chain fatty acids as substrates were discovered in recent years. This article reviews the synthetic potential of aminoacylases to produce biobased N-acyl-amino acid surfactants. The focus lays on a survey of the different types of aminoacylases available for synthesis and their reaction products. The enzymes are categorized according to their protein family classification and their biochemical characteristics including substrate spectra, reaction optima and process stability, both in hydrolysis and under process conditions suitable for synthesis. Finally, the benefits and future challenges of enzymatic N-acyl-amino acid synthesis with aminoacylases will be discussed. KEY POINTS: • Enzymatic synthesis of N-acyl-amino acids, biobased surfactants by aminoacylases.

Indexed as

Amino AcidsBiocatalysisSurface-Active AgentsAmidohydrolasesHydrolysisSubstrate SpecificityAmidohydrolasesAmino AcidsSurface-Active AgentsAminoacylaseBiobased surfactantsBiocatalysisGreen chemistryN-acyl-amino acids

Identifiers

PMID39453420
PMCPMC11511702

What OpenQuestion holds

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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.