Heterologous Production of Pediocin PA-1 in Lactobacillus reuteri

  • Eom, Ji-Eun (Department of Biotechnology, Chungju National University) ;
  • Moon, Sung-Kwon (Department of Biotechnology, Chungju National University) ;
  • Moon, Gi-Seong (Department of Biotechnology, Chungju National University)
  • Received : 2010.03.15
  • Accepted : 2010.05.06
  • Published : 2010.08.28


The recombinant DNA pLR5cat_PSAB, in which pediocin PA-1 structural and immunity genes (pedAB) fused with the promoter and deduced signal sequence of an ${\alpha}$-amylase gene from a bifidobacterial strain were inserted in Escherichia coli-lactobacilli shuttle vector pLR5cat, was transferred to Lactobacillus reuteri KCTC 3679 and the transformant presented bacteriocin activity. The recombinant L. reuteri KCTC 3679 transformed with the shortened pLR5cat(S)_PSAB, where a nonessential region for the lactobacilli replicon was removed, also showed bacteriocin activity. The molecular mass of the secreted pediocin PA-1 from the recombinant bacteria was the same as that of native pediocin PA-1 (~4.6 kDa) from Pediococcus acidilactici K10 on a sodium dodecylsulfate-polyacrylamide gel electrophoresis (SDS-PAGE) gel. In cocultures with Listeria monocytogenes, the recombinant L. reuteri KCTC 3679 effectively reduced the viable cell count of the pathogenic bacterium by a 3 log scale compared with a control where L. monocytogenes was incubated alone.



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