Isolation and characterization of a 67 KDA oligopeptidase from Propionibacterium freudenreichii ATCC 9614
Year: 1998
Type: article
Abstract: 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 α 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 α s1 -CN f1-23 was somewhat different from that of the 44 kDa endopeptidase from the same strain of Propionibacterium and from lactococcal oligopeptidase. The enzyme was strongly inhibited by metal chelators and partially by p-chloromercuribenzoate. The Propionibacterium oligopeptidase was markedly less inhibited by β-CN f58-72 than lactococcal 70 kDa oligopeptidase. The enzyme was most active at pH 6.7-7.5 and at 40°C, but it retained >20% of maximal activity at 7°C and pH 5.5 indicating that it may be active during cheese ripening.
Language: English
Subfield: Biotechnology
Domain: Life Sciences
Open Access status: gold
OpenAlex ID: W2523142958