Abstract
Bacteriocins are antimicrobial peptides that possess a number of desirable properties that can be utilized for application in various industries including the food and pharmaceutical industries. Enterocin NKR-5-3B (Ent53B) and lacticin Q (LnqQ) are well characterized bacteriocins that exhibit exceptional stability and potent antimicrobial activity. Here we report the establishment of a dual-plasmid expression system of these bacteriocins by exploiting the quorum sensing production system of nisin known as the nisin inducible controlled expression (NICETM) system. Using this dual-plasmid expression system, the production of Ent53B and LnqQ can be controlled by the addition of exogenous nisin at sub-lethal concentration, either in pure or crude form, to induce the transcription of the genes responsible for the production of these bacteriocins. Using this system, cheap cultivation media instead of the commonly used complex and expensive cultivation media, can be utilized in the production of these bacteriocins thereby significantly lowering the production cost – one of the major limiting factors for its large-scale application. Additionally, this system provides a robust control of bacteriocin production thereby creating an effective bacteriocin application delivery system.
Highlights
Bacteriocins are antimicrobial peptides produced by diverse bacterial strains as primary metabolites in order for them to gain advantage in their ecological niche (Perez et al, 2014, Klaenhammer, 1993)
We recently reported two novel bacteriocins possessing exceptional properties that could be of high industrial relevance, the bacteriocins enterocin NKR-5-3B (Ent53B) and lacticin Q (LnqQ)
The respective gene encoding the precursor peptides of Ent53B and LnqQ is cloned upstream the nisA promoter region of the theta-replicating plasmid pILPnis while the cognate biosynthetic gene cluster of these bacteriocins are encoded in a rolling-circle plasmid pMG36c carrying a constitutive promoter P32 (Fig. 1)
Summary
Bacteriocins are antimicrobial peptides produced by diverse bacterial strains as primary metabolites in order for them to gain advantage in their ecological niche (Perez et al, 2014, Klaenhammer, 1993). The sub-inhibitory amounts of extracellular nisin is transduced by autophosphorylation of NisR and subsequent phospho-transfer to NisR, triggering the transcription of the genes under the control of nisA and nisF promoters (de Ruyter et al, 1996a) As application to this quorum sensing expression system of nisin biosynthesis, a nisin-inducible expression system (NICETM system) has been developed (de Ruyter et al, 1996b). These enzymes provide the secretion and self-immunity mechanisms of the producer strain to synthesize the LnqQ, which is encoded by the gene lnqQ (Iwatani et al, 2012) In this present study, we report the establishment of a dual-plasmid heterologous expression system that offers a tight control of the production of Ent53B and LnqQ.
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