Antibacterial activity and mechanisms of α-terpineol against foodborne pathogenic bacteria.
Appl Microbiol Biotechnol
; 107(21): 6641-6653, 2023 Nov.
Article
em En
| MEDLINE
| ID: mdl-37682300
ABSTRACT
This study aimed to evaluate the antibacterial activities of α-terpineol against common foodborne pathogenic bacteria by agar well diffusion, broth microdilution, and colony counting assay. Propulsive research was conducted to reveal the antibacterial mechanisms, including morphology, infrared spectroscopy, membrane fluidity, membrane permeability, proton motive force, and oxidative phosphorylation. Results indicated that the antibacterial activity of α-terpineol decreased in the following order Escherichia coli O157H7, Salmonella typhimurium, Listeria monocytogenes, and Staphylococcus aureus. With an initial cell count of 8 log CFU/mL, α-terpineol at 0.8% (v/v) reduced E. coli O157H7 and S. aureus by approximately 5.6 and 3.9 log CFU/mL within 1 h, respectively. Remarkable destruction in cell envelopes and intracellular organizations was observed. The hydroxyl of α-terpineol might form glycosidic bonds with carbohydrates and hydrogen bonds with PO2- and COO- via infrared spectroscopy analysis. Generalized polarization of Laurdan revealed that the polar head groups of phospholipids transformed into close packed. The anisotropy variations of trimethyl amino-diphenylhexatriene (TMA-DPH) and DPH suggested membrane fluidity decreased. The N-phenyl-1-naphthylamine intake assay indicated that α-terpineol impaired the cell wall. Propidium iodide staining was indicative of damaged plasma membranes. Electron transport in the cytoplasmic membrane was impaired, inducing reactive oxygen species accumulation. Both membrane electrical potential and membrane pH gradient collapsed. The disruption of proton motive force and the leakage of ATP resulted in a deficit of intracellular ATP. Our research revealed the interaction between the hydroxyl group of α-terpineol and bacteria affects membrane function contributing to the bacteria's death. KEY POINTS ⢠α-Terpineol hydroxy formed glycosidic bonds and hydrogen bonds with bacteria ⢠α-Terpineol increased the membrane gelation and reduced the membrane fluidity ⢠Proton motive force and oxidative phosphorylation were impaired.
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Base de dados:
MEDLINE
Assunto principal:
Escherichia coli O157
/
Listeria monocytogenes
Idioma:
En
Ano de publicação:
2023
Tipo de documento:
Article