This short review highlights the complete absence of literature on lysins of bacteriophages infecting species like S. salivarius subsp. thermophilus, Pediococcus and Leuconostoc species, L. helveticus, L. acidophilus, L. plantarum and L. brevis, which are also widely used in the dairy industry. The lysins described share some similar biochemical characteristics : optimal pH and temperature, site of hydrolysis inside the peptidoglycan, and some activators and inhibitors. The cloning of the genes encoding these lysins only began in the last few years and four of them have been completely sequenced. In the future, these lysin genes could be interestingly compared to the host autolysin(s) gene(s). By contrast, the passage of phage lysins through the cytoplasmic membrane of the host cell in order to reach the peptidoglycan (via a signal sequence or the presence of a holin) seems not to be clearly resolved. The presence of a second open-reading frame upstream from the gene of the lysin, enabling a putative holin to be encoded, has already been suggested. No doubt our ever increasing knowledge about bacteriophage genome organization will help to elucidate this question. Meanwhile the obtention of a Lactococcus strain with an autolytic phenotype, using a bacteriophage lysin gene, as well as the successful use of purified PL1 lysin to obtain protoplasts of L. casei encourage us to continue to explore the field of bacteriophage lysins.