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Amélioration de la production hétérologue de la bactériocine pédiocine chez Lactococcus lactis

Abstract : Lactococcus lactis is considered an efficient cell factory for recombinant protein production. It is able to produce and secrete class IIa bacteriocins such as pediocin PA-1 via the general secretion (Sec) pathway. However, the positive charges at the N-terminus of pediocin PA-1 might impair secretion via the Sec secretion pathway and the obtained recombinant pediocin has been described as less potent than the pediocin from the natural producer. The impact of two propeptides on the production yield and on the potency of recombinant pediocins was investigated. The nucleotide sequences encoding the propeptides SD or LEISSTCDA were inserted between the sequence encoding the signal peptide of Usp45 and the structural gene of the mature pediocin PA-1. Both propeptides improved secretion of the recombinant pediocins. Although no major impact on the antibacterial activity of recombinant pediocins was observed, all recombinant bacteriocins produced in L. lactis were less potent than wildtype pediocin. Co-expression of the putative thiol-disulfide oxidoreductase PedC, which is encoded by the pediocin PA-1 operon, with the recombinant pediocins allowed to significantly decrease the minimal inhibitory concentration of the produced bacteriocins. To our knowledge, this report shows for the first time that the propeptides SD or LEISSTCDA lead to an improved secretion of recombinant pediocins with apparently no effect on the antibacterial potency and that PedC plays a major role in the potency of pediocin
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Alexandre Back. Amélioration de la production hétérologue de la bactériocine pédiocine chez Lactococcus lactis. Alimentation et Nutrition. Université de Lorraine, 2014. Français. ⟨NNT : 2014LORR0226⟩. ⟨tel-01751223⟩



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