beta-Alanine is mainly produced by chemical methods in current industrial processes. Here, panD from Corynebacterium glutamicum encoding l-aspartate-alpha-decarboxylase (ADC) was cloned and expressed in Escherichia coli BL21(DE3). ADC (C.g) catalyzes the alpha-decarboxylation of l-aspartate to beta-alanine. The purified ADC (C.g) was optimal at 55 A degrees C and pH 6 with excellent stability at 16-37 A degrees C and pH 4-7. A pH-stat directed, fed-batch feeding strategy was developed for enzymatic synthesis of beta-alanine to keep the pH value within 6-7.2 and thus attenuate substrate inhibition. A maximum conversion of 97.2 % was obtained with an initial 5 g l-aspartate/l and another three feedings of 0.5 % (w/v) l-aspartate at 8 h intervals. The final beta-alanine concentration was 12.85 g/l after 36 h. This is the first study concerning the enzymatic production of beta-alanine by using ADC.