Evidence map›Paper›PMID 27858339›Full record

ReviewWorld journal of microbiology & biotechnology2017

Recent advances and challenges in the heterologous production of microbial nitrilases for biocatalytic applications.

Ludmila Martínková, Lenka Rucká, Jan Nešvera, Miroslav Pátek

Abstract readReview
PubMed Publisher
In one paragraph

Review in World journal of microbiology & biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

14 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Nitrilase GiNIT fromInternational journal of molecular sciences · 2024
    Article
  3. Review
  4. Article
  5. Review
  6. Recent Advances in Enzymes for the Bioremediation of Pollutants.Biochemistry research international · 2021
    Review
  7. Article
  8. Genetic and Functional Diversity of Nitrilases in Agaricomycotina.International journal of molecular sciences · 2019
    Article
  9. Review
  10. Review
  11. Article
  12. Cryo-EM and directed evolution reveal howCommunications biology · 2019
    Article
  13. Article
  14. Article
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

4 authors at 2 institutions in 1 country.

Ludmila MartínkováInstitute of Microbiology of the Czech Academy of Sciences, v.v.i., Vídeňská 1083, 142 20, Prague, Czech Republic. martinko@biomed.cas.cz.
Lenka RuckáInstitute of Microbiology of the Czech Academy of Sciences, v.v.i., Vídeňská 1083, 142 20, Prague, Czech Republic.
Jan NešveraInstitute of Microbiology of the Czech Academy of Sciences, v.v.i., Vídeňská 1083, 142 20, Prague, Czech Republic.
Miroslav PátekInstitute of Microbiology of the Czech Academy of Sciences, v.v.i., Vídeňská 1083, 142 20, Prague, Czech Republic.
Czech Academy of Sciences · CZCzech Academy of Sciences, Institute of Microbiology · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The aim of this study is to review the current state of and highlight the challenges in the production of microbial nitrilases as catalysts for the mild hydrolysis of industrially important nitriles. Together with aldoxime dehydratase, the nitrile-hydrolyzing enzymes (nitrilase, nitrile hydratase) are key enzymes in the aldoxime-nitrile pathway which is widely distributed in bacteria and fungi. The availability of nitrilases has grown significantly over the past decade due to the use of metagenomic and database-mining approaches. Databases contain plenty of putative enzymes of this type, whose overproduction may improve the spectrum and the industrial utility of nitrilases. By exploiting this resource, the number of experimentally verified nitrilases has recently increased to several hundred. We especially focus on the efficient heterologous expression systems that are applicable for the overproduction of wild-type nitrilases and their artificial variants. Biocatalyst forms with industrial potential are also highlighted. The potential industrial applications of nitrilases are classified according to their target products (α-hydroxy acids, α- and β-amino acids, cyano acids, amides). The emerging uses of nitrilases and their subtypes (cyanide hydratases, cyanide dihydratases) in bioremediation is also summarized. The integration of nitrilases with other enzymes into artificial multienzymatic and chemoenzymatic pathways is considered a promising strategy for future applications.

Indexed as

AminohydrolasesBacteriaBacterial ProteinsBiocatalysisBiodegradation, EnvironmentalDatabases, ProteinFungal ProteinsFungiMetagenomicsNitrilesProtein EngineeringRecombinant ProteinsAminohydrolasesBacterial ProteinsFungal ProteinsnitrilaseNitrilesRecombinant ProteinsAldoxime–nitrile pathwayBiocatalytic applicationsDatabase miningHeterologous productionMetagenome miningNitrilase

Identifiers

PMID27858339
OpenAlexW2556138883

What OpenQuestion holds

Textmetadata
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.