L-asparaginase catalyzes the hydrolysis of L-asparagine to L-aspartate and ammonia. In the present study, we describe the production, purification, and preliminary characterization of Dickeya solani L-asparaginase. The purification of L-asparaginase was done using ion-exchange chromatography on HiTrap Q-Sepharose Fast Flow followed by FPLC-gel filtration chromatography on Superdex 75 pg. The presence of the enzyme was confirmed by enzymatic activity measurements along with SDS-PAGE analysis. The purified L-asparaginase was shown to exhibit specificity towards L-asparagine, while being inactive against L-glutamine. This data allows us to suggest that the L-asparaginase from Dickeya solani might be clinically more relevant than, e.g., the L-asparaginase isolated from E. coli which hydrolyzed also L-glutamine and produces L-glutamate, a neurotoxic agent. We also demonstrated that the enzymatic activity was enhanced in the presence of TiO 2 and ZnO nanoparticles, making them good candidates to improve L-asparaginase activity. Indeed, the results obtained show that the TiO 2 nanoparticles increased the activity of L-asparaginase by a factor of 6.0 while the ZnO nanoparticles increased it twice.