Cloning, overexpression, and characterization of a thermostable nitrilase from an Antarctic Pyrococcus sp

Extremophiles. 2017 Sep;21(5):861-869. doi: 10.1007/s00792-017-0948-9. Epub 2017 Jul 25.

Abstract

Nitriles are important chemical building blocks for the synthesis of intermediates in fine chemical and pharmaceutical industries. Here, we report a new highly thermostable nitrilase from an Antarctic Pyrococcus sp. MC-FB, a hyperthermophilic archaeon. A gene that encoded a nitrilase was identified and subsequently cloned and overexpressed in Escherichia coli. The recombinant nitrilase, named NitMC-FB, is active as a homodimer (60 kDa) with an optimal temperature and pH of 90 °C and 7.0, respectively. NitMC-FB hydrolyzes preferentially aromatic nitriles, being the first aromatic nitrilase from an archaeon described so far. The K M and V max parameters were determined to be 13.9 mM and 3.7 μmol/min*mg, respectively, with 2-cyanopyridine as the substrate. Additionally, the recombinant nitrilase is highly thermostable with a half-life of 8 h at 90 °C.

Keywords: Antarctica; Archaeon; Nitrilase; Overexpression; Thermostability.

MeSH terms

  • Aminohydrolases / chemistry
  • Aminohydrolases / genetics*
  • Aminohydrolases / metabolism
  • Antarctic Regions
  • Archaeal Proteins / chemistry
  • Archaeal Proteins / genetics
  • Archaeal Proteins / metabolism*
  • Enzyme Stability
  • Protein Denaturation
  • Pyrococcus / enzymology*
  • Pyrococcus / genetics

Substances

  • Archaeal Proteins
  • Aminohydrolases
  • nitrilase