Isolation And Characterization Of A 67 Kda Oligopeptidase From Propionibacterium Freudenreichii Atcc 9614

A non-caseolytic oligopeptidase from the intracellular fraction of Propionibacterium freudenreichii ATCC was purified to homogeneity by chromatography on Fast Q Sepharose, hydroxyapatite and Mono Q. The enzyme was a monomer of molecular mass approximately 67 kDa determined by SDS-PAGE. At similar activity on bradykinin, the enzyme was less active on alpha(s1)-casein (CN) fragments 1-23 and 165-199 and on oxidized insulin chain B than the 70 kDa oligopeptidase from Lactococcus. The specificity of the enzyme on alpha(s1)-CN fl-23 was somewhat