Purification and properties of D-hydantoin hydrolase and N-carbamoyl-D-amino acid amidohydrolase from Flavobacterium sp AJ11199 and Pasteurella sp AJ11221

We characterized recombinant D-hydantoin hydrolase (DHHase) and N-carbamoyl-D-amino acid amidohydrolase (DCHase) from Flavobacterium sp. AJ11199 and Pasteurella sp. AJ11221. The DHHases from these two strains showed a wide range of hydrolytic activity for various 5-monosubstituted D-hydantoin compounds, including a very high level activity for D-hydantoin compounds corresponding to D-aromatic amino acids such as D-tryptophan D-phenylalanine and D-tyrosine. The DCHases, in turn, were capable of catalyzing the hydrolysis of various N-carbamoyi-D-amino acids (NCD-A.A.) corresponding to D-aliphatic and D-aromatic amino acids. The combination of these enzymes was found to be applicable for the production of various D-amino acids. (c) 2004 Elsevier B.V. All rights reserved.