A new d-aminoacylase from Defluvibacter sp. A 131-3

A new d-aminoacylase was found from Defluvibacter sp. A 131-3. It was purified to homogeneity with an overall yield of 37%. This enzyme was specific to N-acyl-d-amino acids, and the activity on N-acetyl-d-valine was higher than that of the other N-acyl-d-amino acids. The enzyme activity was inhibited with CoCl2, NiCl2, MnCl2, and ZnCl2. Optimum pH and temperature were 8.0 and 37 °C, respectively. This enzyme is monomeric with a molecular mass of 56 kDa and an isoelectric point of 5.3. The NH2-terminal sequence similarity was less than 30% of the previously reported d-aminoacylase. This enzyme has great potential for production of d-valine.