Type II L-asparaginase as a pivotal enzyme agent has been applied to treating for acute lymphoblastic leukemia (ALL) and efficient mitigation of acrylamide formed in fried and baked foods. However, low activity, narrow range of pH stability, as well as undesirable glutaminase activity hinder the applications of this enzyme. In our work, A novel type II L-asparaginase (CgASNase) from Corynebacterium glutamicum with molecular mass of about 35 kDa was chosen to express in E. coli. CgASNase shared only 27 % structural identity with the reported L-asparaginase from Helicobacter pylori. The purified CgASNase showed the highest specific activity of 1979.08 IU mg-1 to L-asparagine, compared with reported type II ASNases in the literature. CgASNase displayed superior stability at a wide pH range from 5.0 to 11.0, and retained about 76 % of its activity at 30 ? for 30 min. The kinetic parameters Km (Michaelis constant), k(cat) (turnover number), and k(cat)/K-m (catalytic efficiency) values of 4.66 mM, 79,697.40 min(-1), and 17,102.45 mM(-1) min(-1), respectively. More importantly, CgASNase exhibited strict substrate specificity towards L-asparagine, no detectable activity to L-glutamine. To explore its ability to catalyze L-asparagine, CgASNase was supplied in frying potato chips, which produced the fries with 84 % less acrylamide content compared with no supply. These findings suggest that CgASNase presents excellent properties for chemotherapy against diseases and great potential in the food processing industry.
