Abstract
With the mold acylase preparation, optimal pH and relative activity to the various acyl amino acids were investigated. As a result, a difference of optimal pH was observed between acetyl and chioroacetyl derivatives. A comparison of the susceptibility disclosed that mold preparation has either a wider or loose specificity than renal acylase. Namely, besides aliphatic amino acids, the acyl derivatives of basic amino acids and aromatic amino acids were readily hydrolyzed by the mold preparation. These results indicate that the mold acylase preparation can be used for the resolution of a great variety of amino acids. As an example of this, the resolution of acetyl-DL-tryptophan was presented.
