Abstract
For the purpose of investigating the formation of ε-lysine activity in molds, especially, Aspergillus oryzae was studied, from which it was found to be an inducible enzyme system whose activity is undetectable without induction.
The respective activities inducted with ε-benzoyl-L-, -D-, and -DL-lysines are capable of hydrolyzing both optical isomers of ε-benzoyllysine regardless of the optical nature of the inducers employed.
Several enzymatic properties of this fungal ε-lysine acylase are also presented.
