Abstract
Divercin V41 is a class IIa bacteriocin produced by Carnobacterium divergens V41 with a strong anti-Listeria activity. We have previously produced a recombinant form of divercin V41 (DvnRV41) in Escherichia coli strain Origami, by cloning a synthetic gene that codes for a mature divercin RV41 peptide. In this work we describe the inducible expression and secretion of DvnRV41 in the food-grade lactic acid bacterium, Lactococcus lactis. The production of DvnRV41 by recombinant L. lactis was confirmed and quantified by Western blot and ELISA assays. In addition, anti-Listeria activity of DvnRV41 was determined using an agar diffusion test. Although the levels of DvnRV41 produced by recombinant L. lactis were similar to those produced by the natural host, C. divergens V41, the specific activities were lower. In conclusion, our data show that the bacteriocin DvnRV41 is produced and secreted in an active form by L. lactis and that this approach may have important applications in the preservation of foods.
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