Paper Title
Characterization of crude Nitrilase Produced by Acinetobacter Spin Submereged Fermentation

Abstract
Nitrilases (E.C. 3.5.5.1) are enzymes found abundantly across various organisms, facilitating the hydrolysis of nitrile compounds—a cyano moiety prevalent in additives for pharmaceuticals, agriculture, textiles, chemicals, and other industries—into carboxylic acids and ammonia. While numerous organisms are known to produce nitrilases, only a selected few exhibit properties suitable for industrial applications. Therefore, continued research and development are essential to identify and enhance the industrial potential of these enzymes. In this study, characterization of crude nitrilase enzyme produced by Acinetobacter sp was attemptedby investigating the effect of temperature, pH, different metal ions and substrate type (acetonitrile, benzamide and pyridine) on the activity of the nitrilase. The results revealed that the crude nitrilase had highest activities of 17.72U/mL and 14.1U/mL at 60 °C and pH 6.0 respectively. Effect of metal ions showed that Fe2+, CU2+, Mg2+, Zn2+, Na+, K+ Mn2+, Fe3+ enhanced the activity of the crude nitrilase while Hg+ had a slight inhibitory effect on the enzyme. Effect of different substrate type revealed on nitrilase activity that the crude nitrilase from Acinetobacter sp had activities of 22.83U/mL, 22.61U/mL and 9.87U/mL with acetonitrile, benzamide and pyridineas substrate respectively.These findings underscore the potential of the crude nitrilase enzyme from Acinetobacter sp. for industrial applications, particularly due to its robust activity across varying temperatures, pH levels, metal ions, and substrate types, highlighting the need for further exploration and optimization of such biocatalysts for enhanced industrial utility Keywords - Nitrilase, Temperature, pH, Enzyme, Characterization, Acetonitrile