Physicochemical stability of antilisterial proteins from P. polymyxa Kp10 as potential food biopreservative

Listeria monocytogenes has continuously become a significant threat to consumers worldwide. The use of chemical-derived preservatives that are commonly associated with safety and nutritional issues has prompted the use of natural-based preservatives as a better alternative. Many bacterial strains including Paenibacillus polymyxa Kp10 have been reported to produce various antimicrobial proteins and compounds that are considered more natural. However, their stability in various physicochemical conditions should be examined before being applied in various types of food. In this study, the stability of four previously identified antilisterial proteins in P. polymyxa Kp10 upon exposure to several physicochemical conditions was examined. More than 80% residual antilisterial activity is conserved upon heat and proteinase K treatment. But, sensitivity to 24 h trypsin digestion has been observed. P1 and P2 proteins (histone-like DNA binding proteins HU) were sensitive to alkaline pH (pH 10-12) as compared with other proteins. More than 70% and 97% residual antilisterial activity were recovered after incubation in raw beef homogenates and simulated meat gravy model, respectively. However, the antilisterial activity of most proteins was highly compromised in chicken and salmon meat homogenates, and UHT cow milk. Inoculation of these proteins into Listeria-contaminated simulated meat gravy showed that all proteins exerted a bactericidal action against L. monocytogenes. P1 and P2 shared almost similar antilisterial activity rates, while P4 was the most potent antilisterial protein. The findings in this study could provide important preliminary data for future applications of these proteins as preservative in food products especially beef-based meat products.