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Abstract

A thermostable bacterial 3-cyanopyridinase enzyme has been identified that catalyze 3-cyanopyridine to nicotinic acid and ammonia. Nicotinic acid is mainly used in food, pharmaceutical and biochemical industries. This study was undertaken to optimize the purification of 3-cyanopyridinase enzyme and characterization of its various kinetic properties. The partial purification of enzyme has been carried out in five steps that results in approximately 2.3 fold increased purification with 46.5 % of enzyme recovery. The partially purified enzyme was observed approximately 43 kDa of maximum activity at 50 °C temperature and pH 7.0. The partially purified enzyme showed the K m of 0.91 mM and maximum velocity (V max ) of 0.59 U. The half-life (t 1/2 ) of partially purified enzyme was about 60 min at optimal conditions. The enzyme has broad substrate specificity, hydrolyzing toxic compounds such as benzonitrile and propionitrile. Thus this novel enzyme has potential in bioremediation process.