Characterization of recombinant aminoacylase from Escherichia coli

Abstract

In this study, we report on characterization of the recombinant intracellular aminoacylase from E. coli LGE36 with high levels of aminoacylase activity and wide substrate specificity. The E. coli aminoacylase showed higher activity towards α-N-acetyl-L-ornithine and α-N-acetyl-L-lysine rather than towards N-acetyl-L-methionine. The comparison of the substrate specificity of the recombinant intracellular aminoacylase from E. coli with other members of the aminoacylase family suggests an origin of the obtained enzyme.