详细信息
Anti-Salmonella Activity of a Novel Peptide, KGGDLGLFEPTL, Derived from Egg Yolk Hydrolysate ( SCI-EXPANDED收录) 被引量:1
文献类型:期刊文献
英文题名:Anti-Salmonella Activity of a Novel Peptide, KGGDLGLFEPTL, Derived from Egg Yolk Hydrolysate
作者:Pimchan, Thippawan Tian, Fu Thumanu, Kanjana Rodtong, Sureelak Yongsawatdigul, Jirawat Fodor, Andras
第一作者:Pimchan, Thippawan
通信作者:Yongsawatdigul, J[1]
机构:[1]Suranaree Univ Technol, Inst Agr Technol, Sch Food Technol, Nakhon Ratchasima 30000, Thailand;[2]Guizhou Inst Technol, Coll Food & Pharmaceut Engn, Guiyang 550003, Peoples R China;[3]Synchrotron Light Res Inst Publ Org, Nakhon Ratchasima 30000, Thailand;[4]Suranaree Univ Technol, Inst Sci, Sch Preclin Sci, Nakhon Ratchasima 30000, Thailand
第一机构:Suranaree Univ Technol, Inst Agr Technol, Sch Food Technol, Nakhon Ratchasima 30000, Thailand
通信机构:corresponding author), Suranaree Univ Technol, Inst Agr Technol, Sch Food Technol, Nakhon Ratchasima 30000, Thailand.
年份:2024
卷号:13
期号:1
外文期刊名:ANTIBIOTICS-BASEL
收录:;Scopus(收录号:2-s2.0-85183373182);WOS:【SCI-EXPANDED(收录号:WOS:001151907800001)】;
基金:No Statement Available
语种:英文
外文关键词:egg yolk protein; antimicrobial peptide; food-borne pathogens; Salmonella Typhimurium
摘要: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 Salmonella enterica serovar Typhimurium TISTR 292 and S. enterica serovar Enteritidis DMST 15679 with a MIC value of 2 mM. In contrast, S. enterica serovar Newport ATCC 6962 and other strains of Typhimurium and Enteritidis were inhibited at 4 mM. EYHp6 increased the cell membrane permeability of S. 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 x MIC induced disruption of cell membranes. Electron microscopy revealed that treatment of S. 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 S. 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 S. enterica.
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