Article Abstract:
Researchers have developed antibodies against bacteriocins that could be used to detect and quantify bacteriocins in food. Bacteriocins produced by lactic acid bacteria are believed to be natural food preservatives. The antibodies show that Lactococcus lactis produces at least two bacteriocins, enterocin A and pediocin PA-1.
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Article Abstract:
Pediocin PA-1 from Pediococcus acidilactici and lactococcin A from Lactococcus lactis subsp. lactis bv. diacetylactis share many common features. Both class II bacteriocins are produced as precursor peptides with the same amino-terminal leader sequences having a conserved processing site. Their translocation both occur through a dedicated secretory system. The lactococcin A secretory system was adapted for the expression and secretion of pediocin PA-1 in L. lactis IL1403, with the resulting L. lactis strains secreting a bacteriocin with about 25% of the antimicrobial activity shown by the parental pediocin-producing P. acidilactici 347.
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Article Abstract:
Rabbit polyclonal antibodies, with specificity for against a chemically synthesized C-terminal fragment of the bacteriocin (PH2) pediocin PA-1, were developed. This was accomplished through the immunization of rabbits with a PH2 conjugated to the carrier protein keyhole limpet hemocyanin (KLH). The sensitivity and specificity of the PH2-KLH-produced antibodies were proven by various enzyme-linked immunosorbent assays.
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