Enzymatic Resolution of Racemic Amino Acids

Part IV. Another Purification Method of Mold Acylase and Effect of Metal Ions, Cyanide and EDTA on the Enzyme Activity

Abstract

The mold acylase has been purified by precipitation of the enzyme-rivanol complex and elution from the complex, together with fractionation with ammonium sulfate and acetone.
The mold acylase appears to be specifically activated by Co⁺⁺ ion and inactivated by Mn⁺⁺ and Hg⁺⁺ ions as well as by EDTA.
The enzyme activity inhibited by EDTA was restored to its original level with the addition of the cobaltous ion.
This research was aided by a grant from the Ajinomoto Company.