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The antibacterial mechanism of ultrasound in combination with sodium hypochlorite in the control of Escherichia coli

文献类型： 外文期刊

作者： Guo, Liping 1 ; Sun, Yongcai 1 ; Zhu, Yinglian 1 ; Wang, Baowei 1 ; Xu, Lin 1 ; Huang, Ming 3 ; Li, Yufeng 4 ; Sun, Jingx 1 ;

作者机构： 1.Qingdao Agr Univ, Coll Food Sci & Engn, Qingdao 266109, Shandong, Peoples R China

2.Qingdao Agr Univ, Shandong Reseach Ctr Meat Food Qual Control, Qingdao 266109, Shandong, Peoples R China

3.Nanjing Agr Univ, Nanjing Innovat Ctr Meat Prod Proc, Nanjing 210095, Jiangsu, Peoples R China

4.Shandong Acad Agr Sci, Poultry Inst, Jinan 250023, Shandong, Peoples R China

关键词： Ultrasound; Sodium hypochlorite; Escherichia coli; Combined treatment; Antibacterial

期刊名称：FOOD RESEARCH INTERNATIONAL （ 影响因子：6.475； 五年影响因子：6.508 ）

ISSN： 0963-9969

年卷期： 2020 年 129 卷

页码：

收录情况： SCI

摘要： In the present study, the action mechanism of ultrasound (US) combined with sodium hypochlorite (SH) against Escherichia colt was illustrated by different analysis, including reduction, particle size distribution, scanning electron microscopy (SEM), transmission electron microscopy (TEM), K+ leakage, confocal laser scanning microscopy (CISM) and fluorescence spectroscopy of Escherichia coli. The results showed that ultrasound improved the antimicrobial effect of SH in control of E. coli. No significant difference was obtained in reduction of E. coli, CLSM analysis and K+ leakage between US + SH30 (US + 30 ppm SH) and SH50 (50 ppm SH) treatment. Smaller particle size was recorded in US and US + SH30 treatment. The changes of morphology and intracellular organization of E. coli cells as a result of these treatments were confirmed by SEM and TEM analyses. Fluorescence spectroscopy results indicated Slim US + SH30 and SH50 treatment caused the burial of tyrosine residues and tryptophan residues as well as increase of hydrophobicity. Therefore, the mechanism of US + SH30 treatment against E. coli involved decreased particle size, damaged membrane and changes of intracellular organization and protein conformation.

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