Biotransformation has accompanied mankind since the Neolithic community, when people settled down and began to engage in agriculture [...].

• MeSH
• Bacteria enzymology   MeSH
• Biocatalysis * MeSH
• Biosensing Techniques MeSH
• Biotransformation MeSH
• Glycomics MeSH
• Fungi enzymology   MeSH
• Humans MeSH
• Agriculture MeSH
• Check Tag
• Humans MeSH
• Publication type
• Introductory Journal Article MeSH
• Editorial MeSH

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.

• Keywords
• Aldoxime–nitrile pathway, Biocatalytic applications, Database mining, Heterologous production, Metagenome mining, Nitrilase,
• MeSH
• Aminohydrolases genetics   metabolism   MeSH
• Bacteria enzymology   genetics   MeSH
• Bacterial Proteins genetics   metabolism   MeSH
• Biodegradation, Environmental MeSH
• Biocatalysis MeSH
• Databases, Protein MeSH
• Fungal Proteins genetics   metabolism   MeSH
• Fungi enzymology   genetics   MeSH
• Metagenomics MeSH
• Nitriles metabolism   MeSH
• Protein Engineering methods   MeSH
• Recombinant Proteins metabolism   MeSH
• Publication type
• Journal Article MeSH
• Review MeSH
• Names of Substances
• Aminohydrolases MeSH
• Bacterial Proteins MeSH
• Fungal Proteins MeSH
• nitrilase MeSH Browser
• Nitriles MeSH
• Recombinant Proteins MeSH

We announce the completion of the genome sequence of a phenol derivative-degrading bacterium, Rhodococcus erythropolis strain CCM2595. This bacterium is interesting in the context of bioremediation for its capability to degrade phenol, catechol, resorcinol, hydroxybenzoate, hydroquinone, p-chlorophenol, p-nitrophenol, pyrimidines, and sterols.

• Publication type
• Journal Article MeSH

Escherichia coli strains expressing different nitrilases transformed nitriles or KCN. Six nitrilases (from Aspergillus niger (2), A. oryzae, Neurospora crassa, Arthroderma benhamiae, and Nectria haematococca) were arylacetonitrilases, two enzymes (from A. niger and Penicillium chrysogenum) were cyanide hydratases and the others (from P. chrysogenum, P. marneffei, Gibberella moniliformis, Meyerozyma guilliermondi, Rhodococcus rhodochrous, and R. ruber) preferred (hetero)aromatic nitriles as substrates. Promising nitrilases for the transformation of industrially important substrates were found: the nitrilase from R. ruber for 3-cyanopyridine, 4-cyanopyridine and bromoxynil, the nitrilases from N. crassa and A. niger for (R,S)-mandelonitrile, and the cyanide hydratase from A. niger for KCN and 2-cyanopyridine.

• MeSH
• Aminohydrolases chemistry   genetics   metabolism   MeSH
• Hydro-Lyases chemistry   genetics   metabolism   MeSH
• Escherichia coli genetics   MeSH
• Fungal Proteins chemistry   genetics   metabolism   MeSH
• Genome, Fungal * MeSH
• Genomics MeSH
• Fungi enzymology   genetics   MeSH
• Recombinant Proteins chemistry   genetics   metabolism   MeSH
• Sequence Analysis, DNA MeSH
• Sequence Homology, Amino Acid MeSH
• Sequence Alignment MeSH
• Substrate Specificity MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Comparative Study MeSH
• Names of Substances
• Aminohydrolases MeSH
• cyanide hydratase MeSH Browser
• Hydro-Lyases MeSH
• Fungal Proteins MeSH
• nitrilase MeSH Browser
• Recombinant Proteins MeSH