Heterologous Expression of Pediocin PA-1 in Escherichia coli

Abstract Pediocin PA-1 is an antimicrobial peptide which has a strongly activity against some Gram – positive pathogens such as Listeria monocytogenes, Staphylococcus aureus, Enterococcus faecalis… With the broad inhibitory spectrum as well as pH and temperature stability, pediocin has a potential application in food preservation as well as pharmaceutical industry. For higher manufactory efficiency, pediocin has been expressed in both prokaryote and eukaryote heterologous expression system, mostly on Escherichia coli with different strategies. Here, we show a new strategy to produce pediocin from Escherichia coli BL21(DE3) system as fusion form by using a vector containing NusA tag. Our results showed that NusA fused pediocin almost presented in soluble form with high efficiency (79.8 mg/l obtained by Ni-NTA purification). After remove the fusion tag, recombinant pediocin showed antimicrobial activity against Listeria monocytogenes ATCC 13932 as 23.5×10 3 Au/mg as well as against Enterococcus faecalis, Lactobacillus plantarum, and Streptococcus thermophilus , especially Vibrio parahaemolyticus – a Gram-negative bacteria which have not been reported in antimicrobial spectrum of pediocin on Bactibase. Recombinant pediocin is recorded to be stable to a wide range of pH (1-12 for 1 hour) and temperature (100°C for 15 min) as well as sensitive to protease treatment as the nature pediocin. These characteristics opened a prospect of using pediocin as bio-preservative compound in food industry.