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A peptidase showing a high level of specificity towards dipeptides of the X-Pro type was purified to homogeneity from the cell extract of Lactobacillus casei subsp. casei IFPL 731. The enzyme was a monomer having a molecular mass of 41 kDa. The pH and temperature optima were 6.5 to 7.5 and 55؇C, respectively. Metal chelating agents completely inhibited enzyme activity, indicating that the prolidase was a metalloenzyme. The Michaelis constant (K m) and V max for several proline-containing dipeptides were determined.

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