Purification and Properties of D-Aminoacylase of Streptomyces olivaceus

Abstract

D-Aminoacylase for enzymatic resolution of DL-amino acids was produced in the presence of inducer by Streptomyces olivaceus and almost all the activity was found in cell fraction. The partial purification and properties of this induced enzyme were studied. The enzyme had a molecular weight of about 45, 000 and was specific for the hydrolysis of N-acetyl D-amino acids. The optimum pH was found to be at pH 7.0 and the activity was remarkably inhibited by the presence of Hg²⁺ or Ago²⁺. Enzyme stability was increased by the addition of Co²⁺. Michaelis constants (Km) for several preferred substrates were between 1.13×10^-3 and 2.95×10^-3M.