Pediocin PA-1, mainly produced from Pediococcus spp., is a well-known class IIa bacteriocin showing strong anti-listerial activity. Pediococcus acidilactici K10 producing the bacteriocin was transformed with pLR5cat(S)_PSAB in which the pediocin PA-1 structural gene (pedA) was translationally fused with a deduced signal sequence of the bifidobacterial ${alpha}$-amylase gene for secretion. The P. acidilactici K10 transformant presented increased bacteriocin activity when compared with that of native P. acidilactici K10. The P. acidilactici K10 mutant (K10M), in which the plasmid for pediocin PA-1 production is cured, also showed bacteriocin activity when transformed with pLR5cat(S)_PSAB, indicating that the pediocin gene was expressed in hosts. An increase in pedA gene transcription level and the detection of both transcripts from the pediocin operon and PSAB were also confirmed. The P. acidilactici K10 [pLR5cat(S)_PSAB] transformant was more inhibitory against Listeria monocytogenes than that of the P. acidilactici K10 wild type in co-cultures.