Protein variations in Listeria monocytogenes exposed to sodium lactate, sodium diacetate, and their combination

Abstract

Most studies of the effect of adverse conditions on survival of Listeria monocytogenes have focused on stress caused by acid or sodium chloride. However, no information is available on resistance of this pathogen to stress caused by salts of organic acids. Sodium lactate and sodium diacetate are generally recognized as safe substances and are approved as ingredients for use in foods. We evaluated antilisterial properties of each of these salts and the enhanced inhibition effected by their combination in ready-to-eat meat products at pH 6.3. Changes in proteins found in this pathogen were studied in the presence of the salts in a chemically defined medium at the same pH using a proteomic approach. The total numbers of protein spots obtained from two-dimensional electrophoresis were 198, 150, and 131 for sodium diacetate, sodium lactate, and the control, respectively. Sodium diacetate treatment produced the highest number of unmatched proteins (124 versus 53 in lactate), the greatest increase in expression (20 versus 5 in lactate), and the highest number of novel proteins (90 versus 45 in lactate). The number of repressed proteins was highest in the combination treatment (41 versus ∼ 30 in the single salt treatment). Six proteins that increased or decreased by ≥ 10-fold were further investigated; oxidoreductase and lipoprotein were upregulated, and DNA-binding protein, alpha amylase, and two SecA proteins were downregulated or completely suppressed by the salt treatment. Identification of all protein spots is essential for comparison with proteins induced or suppressed under other stress conditions. Copyright ©, International Association for Food Protection.