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A peptidase gene expressingl -proline-β-naphthylamide-hydrolyzing activity was cloned from a gene library ofLactobacillus rhamnosus 1/6 isolated from cheese. Peptidase-expressing activity was localized in a 1.5-kbSac I fragment. A sequence analysis of theSac I fragment revealed the presence of one complete open reading frame (ORF1) that was 903 nucleotides long. The ORF1-encoded 34.2-kDa protein exhibited 68% identity with the PepR protein fromLactobacillus helveticus . Additional sequencing revealed the presence of another open reading frame (ORF2) followingpepR ; this open reading frame was 459 bp long. Northern (RNA) and primer extension analyses indicated thatpepR is expressed both as a monocistronic transcriptional unit and as a dicistronic transcriptional unit with ORF2. Gene replacement was used to construct a PepR-negative strain ofL. rhamnosus . PepR was shown to be the primary enzyme capable of hydrolyzing Pro-Leu inL. rhamnosus . However, the PepR-negative mutant did not differ from the wild type in its ability to grow and produce acid in milk. The clonedpepR expressed activity against dipeptides with N-terminal proline residues. Also, Met-Ala, Leu-Leu, and Leu-Gly-Gly and the chromogenic substratesl -leucine-β-naphthylamide andl -phenylalanine-β-naphthylamide were hydrolyzed by the PepR ofL. rhamnosus .

Cloning and Characterization of a Prolinase Gene ( pepR ) from Lactobacillus rhamnosus