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From sequence to function: a new workflow for nitrilase identification.

Richard Egelkamp1, Ines Friedrich1, Robert Hertel1

  • 1Genomic and Applied Microbiology & Göttingen Genomics Laboratory, Institute of Microbiology and Genetics, Georg-August-University of Göttingen, Grisebachstraße 8, 37077, Göttingen, Germany.

Applied Microbiology and Biotechnology
|April 16, 2020
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Summary
This summary is machine-generated.

Researchers developed a rapid, high-throughput assay for identifying active nitrilases from metagenomes. This method enabled the discovery and detailed characterization of a novel, stable arylacetonitrilase enzyme.

Keywords:
ArylacetonitrilaseMetagenomeNitrilaseNitrilase assayPhenylacetonitrile

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Area of Science:

  • Biocatalysis
  • Enzymology
  • Metagenomics

Background:

  • Nitrilases are crucial industrial biocatalysts for nitrile degradation.
  • Efficient recovery and screening of novel nitrilases from metagenomic data are challenging.

Purpose of the Study:

  • To develop a simple, fast workflow for recovering and identifying active nitrilase candidates from metagenomes.
  • To characterize novel nitrilases, including their substrate specificity and stability.

Main Methods:

  • Established a NADH-coupled high-throughput assay for direct measurement of nitrile degradation in crude extracts.
  • Screened 70 putative nitrilase genes from metagenomes, assaying 13 candidates.
  • Purified and analyzed a novel arylacetonitrilase (Nit09).

Main Results:

  • The assay successfully identified active nitrilases from crude extracts, omitting purification steps.
  • Six of 13 screened candidates showed nitrilase activity.
  • The novel arylacetonitrilase Nit09 demonstrated broad pH stability and high activity for arylacetonitriles (KM = 1.29 mM, Vmax = 13.85 U/mg).

Conclusions:

  • A rapid and simplified method for analyzing putative nitrilase-encoding genes from sequence to function was established.
  • The workflow facilitated the identification, isolation, and detailed characterization of a novel arylacetonitrilase.