Abstract: L-aspartate-α-decarboxylase gene panD from Corynebacterium glutamicum was cloned and efficiently expressed in Escherichia coli BL21（DE3）. The α and β subunits of PanD were observed by Tris-tricine SDS-PAGE, indicating that the PanD was successful processed by self cleavage. The specific activity of the recombinant enzyme was as high as 2.60 U/mg（156 mmol/g?h）. The optimum temperature was 55℃ and the optimum pH was 7.0. Under the condition of 80℃ , the half-life of PanD was approximately 40 min. Under the condition of 37℃ and pH7.5, the Km value was 4.26 mmol/L, the V_max value was 35.97 nmol/min, the k_cat value was 1.02/s and the catalytic efficiency（k_cat/K_m）was 0.24 L/mmol?s.

Key words: L-aspartate-α-decarboxylase, Corynebacterium glutamicum, Expression, Purification, Enzymatic properties