Peptide Hydrolases of Propionibacteria: Effect of pH and Temperature

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Abstract
A comparative study of the activity of peptidases belonging to the four classic propionibacteria species cultured in milk was carried out at different values of pH and temperature. Leucine aminopeptidase and proline iminopeptidase showed greater activity in Propionibacterium freudenreichii than in the other species studied. With the single exception of Propionibacterium jensenii, the propionibacteria peptidase tested exhibited greater affinity for proline than for leucine-p-nitroanilide. Optimum temperature and pH in relation to the activity of both substrates varied according to the species under consideration.

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