A New Thermophilic Nitrilase from an Antarctic Hyperthermophilic Microorganism

  • Dennett G
  • Blamey J
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Abstract

© 2016 Dennett and Blamey. Several environmental samples from Antarctica were collected and enriched to search for microorganisms with nitrilase activity. A new thermostable nitrilase from a novel hyperthermophilic archaea Pyrococcus sp. M24D13 was purified and characterized. The activity of this enzyme increased as the temperatures rise from 70 up to 85°C. Its optimal activity occurred at 85°C and pH 7.5. This new enzyme shows a remarkable resistance to thermal inactivation retaining more than 50% of its activity even after 8 h of incubation at 85°C. In addition, this nitrilase is highly versatile demonstrating activity toward different substrates, such as benzonitrile (60 mM, aromatic nitrile) and butyronitrile (60 mM, aliphatic nitrile), with a specific activity of 3286.7 U mg-1of protein and 4008.2 U mg-1of protein, respectively. Moreover the enzyme NitM24D13 also presents cyanidase activity. The apparent Michaelis-Menten constant (Km) and Vmáxof this Nitrilase for benzonitrile were 0.3 mM and 333.3 μM min-1, respectively, and the specificity constant (kcat/Km) for benzonitrile was 2.05 × 105s-1M-1.

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Dennett, G. V., & Blamey, J. M. (2016). A New Thermophilic Nitrilase from an Antarctic Hyperthermophilic Microorganism. Frontiers in Bioengineering and Biotechnology, 4. https://doi.org/10.3389/fbioe.2016.00005

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