Anti-Salmonella Activity of a Novel Peptide, KGGDLGLFEPTL, Derived from Egg Yolk Hydrolysate
The present study aimed to characterize the mode of action of a novel antimicrobial peptide isolated from egg yolk hydrolysate. The EYHp6, KGGDLGLFEPTL, exhibited inhibition against <i>Salmonella enterica</i> serovar Typhimurium TISTR 292 and <i>S. enterica</i> serovar Enteri...
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MDPI AG
2023-12-01
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| Series: | Antibiotics |
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| Online Access: | https://www.mdpi.com/2079-6382/13/1/19 |
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| author | Thippawan Pimchan Fu Tian Kanjana Thumanu Sureelak Rodtong Jirawat Yongsawatdigul |
| author_facet | Thippawan Pimchan Fu Tian Kanjana Thumanu Sureelak Rodtong Jirawat Yongsawatdigul |
| author_sort | Thippawan Pimchan |
| collection | DOAJ |
| description | The present study aimed to characterize the mode of action of a novel antimicrobial peptide isolated from egg yolk hydrolysate. The EYHp6, KGGDLGLFEPTL, exhibited inhibition against <i>Salmonella enterica</i> serovar Typhimurium TISTR 292 and <i>S. enterica</i> serovar Enteritidis DMST 15679 with a MIC value of 2 mM. In contrast, <i>S</i>. <i>enterica</i> serovar Newport ATCC 6962 and other strains of Typhimurium and Enteritidis were inhibited at 4 mM. EYHp6 increased the cell membrane permeability of <i>S</i>. Typhimurium TISTR 292, leading to DNA leakage. Membrane integrity determined by propidium iodide and SYTO9 staining visualized by confocal microscopy demonstrated that EYHp6 at 1 × MIC induced disruption of cell membranes. Electron microscopy revealed that treatment of <i>S.</i> Typhimurium with EYHp6 led to damage to the cell membrane, causing the leakage of intracellular contents. Synchrotron-based Fourier-transform infrared spectroscopy indicated that EYHp6 killed <i>S.</i> Typhimurium by targeting fatty acids and nucleic acids in the cell membrane. The peptide did not show hemolytic activity up to 4 mM. These findings suggest that EYHp6 could be a promising antibacterial agent for controlling the growth of <i>S</i>. <i>enterica</i>. |
| first_indexed | 2024-03-08T11:08:00Z |
| format | Article |
| id | doaj.art-f7f0ddab9b51428bb46e1c6b49be6ed9 |
| institution | Directory Open Access Journal |
| issn | 2079-6382 |
| language | English |
| last_indexed | 2024-03-08T11:08:00Z |
| publishDate | 2023-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antibiotics |
| spelling | doaj.art-f7f0ddab9b51428bb46e1c6b49be6ed92024-01-26T14:36:35ZengMDPI AGAntibiotics2079-63822023-12-011311910.3390/antibiotics13010019Anti-Salmonella Activity of a Novel Peptide, KGGDLGLFEPTL, Derived from Egg Yolk HydrolysateThippawan Pimchan0Fu Tian1Kanjana Thumanu2Sureelak Rodtong3Jirawat Yongsawatdigul4School of Food Technology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima 30000, ThailandCollege of Food and Pharmaceutical Engineering, Guizhou Institute of Technology, Guiyang 550003, ChinaSynchrotron Light Research Institute (Public Organization), Nakhon Ratchasima 30000, ThailandSchool of Preclinical Sciences, Institute of Science, Suranaree University of Technology, Nakhon Ratchasima 30000, ThailandSchool of Food Technology, Institute of Agricultural Technology, Suranaree University of Technology, Nakhon Ratchasima 30000, ThailandThe present study aimed to characterize the mode of action of a novel antimicrobial peptide isolated from egg yolk hydrolysate. The EYHp6, KGGDLGLFEPTL, exhibited inhibition against <i>Salmonella enterica</i> serovar Typhimurium TISTR 292 and <i>S. enterica</i> serovar Enteritidis DMST 15679 with a MIC value of 2 mM. In contrast, <i>S</i>. <i>enterica</i> serovar Newport ATCC 6962 and other strains of Typhimurium and Enteritidis were inhibited at 4 mM. EYHp6 increased the cell membrane permeability of <i>S</i>. Typhimurium TISTR 292, leading to DNA leakage. Membrane integrity determined by propidium iodide and SYTO9 staining visualized by confocal microscopy demonstrated that EYHp6 at 1 × MIC induced disruption of cell membranes. Electron microscopy revealed that treatment of <i>S.</i> Typhimurium with EYHp6 led to damage to the cell membrane, causing the leakage of intracellular contents. Synchrotron-based Fourier-transform infrared spectroscopy indicated that EYHp6 killed <i>S.</i> Typhimurium by targeting fatty acids and nucleic acids in the cell membrane. The peptide did not show hemolytic activity up to 4 mM. These findings suggest that EYHp6 could be a promising antibacterial agent for controlling the growth of <i>S</i>. <i>enterica</i>.https://www.mdpi.com/2079-6382/13/1/19egg yolk proteinantimicrobial peptidefood-borne pathogens<i>Salmonella</i> Typhimurium |
| spellingShingle | Thippawan Pimchan Fu Tian Kanjana Thumanu Sureelak Rodtong Jirawat Yongsawatdigul Anti-Salmonella Activity of a Novel Peptide, KGGDLGLFEPTL, Derived from Egg Yolk Hydrolysate Antibiotics egg yolk protein antimicrobial peptide food-borne pathogens <i>Salmonella</i> Typhimurium |
| title | Anti-Salmonella Activity of a Novel Peptide, KGGDLGLFEPTL, Derived from Egg Yolk Hydrolysate |
| title_full | Anti-Salmonella Activity of a Novel Peptide, KGGDLGLFEPTL, Derived from Egg Yolk Hydrolysate |
| title_fullStr | Anti-Salmonella Activity of a Novel Peptide, KGGDLGLFEPTL, Derived from Egg Yolk Hydrolysate |
| title_full_unstemmed | Anti-Salmonella Activity of a Novel Peptide, KGGDLGLFEPTL, Derived from Egg Yolk Hydrolysate |
| title_short | Anti-Salmonella Activity of a Novel Peptide, KGGDLGLFEPTL, Derived from Egg Yolk Hydrolysate |
| title_sort | anti salmonella activity of a novel peptide kggdlglfeptl derived from egg yolk hydrolysate |
| topic | egg yolk protein antimicrobial peptide food-borne pathogens <i>Salmonella</i> Typhimurium |
| url | https://www.mdpi.com/2079-6382/13/1/19 |
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