Applied Microbiology and Biotechnology

, Volume 44, Issue 3–4, pp 386–392 | Cite as

The occurrence of two intracellular oligoendopeptidases in Lactococcus lactis and their significance for peptide conversion in cheese

  • R. Baankreis
  • S. van Schalkwijk
  • A. C. Alting
  • F. A. Exterkate
Biotechnology Original Paper


Two intracellular oligopeptide-preferring endopeptidases have been detected in Lactococcus lactis. A neutral thermolysin-like oligoendopeptidase (NOP) has been purified to homogeneity and an alkaline oligoendopeptidase has been partially purified. The specificity of the oligoendopeptidases towards important intermediary cheese peptides, produced by chymosin action on the caseins, clearly differs from that of the cell-envelope proteinase (CEP). NOP is active under conditions prevailing in cheese and contributes to initial proteolysis in a young cheese. It probably plays a crucial role in the degradation of an important bitter peptide in cheese, the β-casein 193–209 fragment. The relatively low activity of the alkaline endopeptidase is further suppressed in cheese by the highly competitive actions of NOP and CEP.


Peptide Crucial Role Lactis Endopeptidase Lactococcus Lactis 
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Copyright information

© Springer-Verlag 1995

Authors and Affiliations

  • R. Baankreis
    • 1
  • S. van Schalkwijk
    • 1
  • A. C. Alting
    • 1
  • F. A. Exterkate
    • 1
  1. 1.Department of Biophysical ChemistryNetherlands Institute for Dairy Research (NIZO)EdeThe Netherlands

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