Characterization of novel bacteriocin PB2 and comprehensive detection of the pediocin gene ped-A1 from Pediococcus pentosaceus PB2 strain isolated from a sorghum-based fermented beverage in Nigeria

• Published in: Biotechnology reports (Amsterdam, Netherlands) Netherlands), 2022-12, Vol.36, p.e00772-e00772, Article e00772
• Main Authors: Otunba, Ahmed Adebisi, Osuntoki, Akinniyi Adediran, Okunowo, Wahab, Olukoya, Daniel Kolawole, Babalola, Benjamin Ayodipupo
• Format: Article
• Language: English
• Subjects: Bacteriocin PB2; Characterization; Pediococcus pentosaceus PB2; Pito production; Sorghum
• ISSN: 2215-017X; 2215-017X
• DOI: 10.1016/j.btre.2022.e00772

•Novel bacteriocin PB2 was obtained from Pediococcus pentosaceus PB2 strain isolated from fermented sorghum beverage in Nigeria, Pito.•The PB2 isolate exhibited antagonistic activity against E. coli ATCC 25922 and L. monocytogenes ATCC 15313.•The specific activity, purification fold, and recovery yield of bacteriocin PB2 from Carboxymethyl-Sephadex C-50 are 2.65 U/mg, 12.62 and 13.3% respectively.•The bacteriocin PB2 is a proteinous bacteriocidal agent with a molecular weight of 4.87 kDa, with optimum activity at 40 °C and pH 5.0. Bacteriocin PB2 lost its activity on treatment with proteinase K and exposure to UV radiation (after 6 h) but was observed to have stable activity in the presence of organic solvents.•The amplicon size of Pediococcus pentosaceus PB2 was 727 bp. P. pentosaceus was found to harbor two plasmids targeted from primers designed from operon encoding pediocin PA-1 gene. The molecular sizes of the plasmids are 0.9 and 1.2 kb. The curing analysis showed that the bacteriocidal activity of P. pentosaceus is derived from the presence of the plasmid present. Lactic acid bacteria (LAB) have been known to possess bacteriocidal activity resulting from ribosomally synthesized antimicrobial peptides called bacteriocin. This study focused on the characterization of the bactericidal activity of bacteriocin PB2 and comprehensive detection of the pediocin ped-A1 from Pediococcus pentosaceus obtained from fermented sorghum beverage, Pito, in Nigeria against Escherichia coli ATCC 25922 and Listeria monocytogenes ATCC 15313. Bacteriocin PB2 was purified in a 2-step purification using 80% NH4 (SO4)2, and Carboxymethyl-Sephadex G-50 column chromatography to achieve a 12.62% purification fold. The physicochemical properties of purified bacteriocin were characterized being treated at different temperatures (20 – 120 °C), pH (2.0 – 10.0), with different detergents and enzymes (sodium dodecyl sulphate (SDS) urea, ox-gall, and proteinase K and RNase A), organic solvents (ethanol, phenol, acetone, chloroform and isoamyl alcohol), and exposure to ultraviolet (UV) radiation (2–12 h) respectively. The molecular weight of the bacteriocin PB2 was determined to be 4.87 kDa. The antibacterial activity of bacteriocin PB2 was optimum at 40 °C and pH 5.0. The bacteriocin PB2 lost its activity on treatment with proteinase K and exposure to UV radiation (after 6 h) but was observed to have stable activity in the presence of organic solvents. Also, P. pentosaceus PB2 harbored