Abstract
1, The mold acylase of P. uinaceous was prepared by fractionation procedures with 0.6 saturation of ammonium sulfate, acetone precipitation, calcium gel adsorp-ton and following elution with phosphate buffer.
2. The enzymatic susceptibility of N-acylated amino acids and glycylpeptides towards the acylase were studied. The enzyme was more effective towards the acylderivatives of aromatic-substituted amino acids than towards those of
aliphatic amino acids. The enzyme possessed little or no action to hydrolyze the acylated D-amino acids.
3. DL-Phenylalanine and DL-methionine were resolved in relatively good yield by asymmetric hydrolysis of the acetylderi-vatives of these amino acids with the mold acylase.
