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Saturday, 27 February 2016

A new thermophilic nitrilase from Pyrococcus sp. M24D13

A new thermophilic nitrilase from an Antarctic hyperthermophilic microorganism by Geraldine V. Dennett and Jenny M. 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 towards different substrates such as benzonitrile (60 mM, aromatic nitrile) and butyronitrile (60 mM, aliphatic nitrile). Moreover the enzyme NitM24D13 also presents cyanidase activity.

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