Purification and Properties of the Pyrrolidonecarboxylate Peptidase of Streptococcus faecium

Abstract

Pyrrolidonecarboxylate peptidase (BC 3.4.11.8) from Streptococcus faecium was purified by fractionation with streptomycin sulphate and ammonium sulphate, by chromatography on Sephadex G200 and DBAB-cellulose, and by preparative electrophoresis on Sephadex G25. The purified enzyme on acrylamide gel showed a strong protein band which contained enzyme activity and a very faint band which had no activity.