Edhi Nurhartadi , Sureelak Rodtong , Kanjana Thumanu , Si Hong Park , Rotimi E. Aluko , Jirawat Yongsawatdigul
{"title":"Antibacterial activity of enzymatic corn gluten meal hydrolysate and ability to inhibit Staphylococcus aureus in ultra-high temperature processed milk","authors":"Edhi Nurhartadi , Sureelak Rodtong , Kanjana Thumanu , Si Hong Park , Rotimi E. Aluko , Jirawat Yongsawatdigul","doi":"10.1016/j.foodcont.2024.110998","DOIUrl":null,"url":null,"abstract":"<div><div>The aim of this work was to determine the antibacterial properties and mode of activity of isolated corn gluten meal (CGM) hydrolysate fractions. The P1 fraction from reverse-phase liquid chromatography separation of pepsin-hydrolyzed CGM presented the most potent antibacterial activity with minimum inhibitory concentration (MIC) of 1 mM and 4 mM minimum bactericidal concentration (MBC) against <em>Staphylococcus aureus</em> ATCC29213. The kinetics of P1 antibacterial activity revealed a bacteriostatic effect at 1 × MIC and 2 × MIC for 8 h, but a bactericidal effect at 4 × MIC. The P1 fraction at 1 × MIC and 4 × MIC disrupted the membrane integrity of <em>S. aureus</em> after 8 h exposure as observed by confocal laser scanning microscopy. Scanning electron microscopy and transmission electron microscopy indicated cell surface damage and cytoplasmic leakage in <em>S. aureus</em> after being exposed to the P1 fraction. Synchrotron radiation-Fourier transmission infrared (SR-FTIR) microspectroscopy revealed changes in nucleic acid, protein, and fatty acid compositions of <em>S. aureus</em> cell membrane after 8 h exposure to P1 at 1 × MIC. The antibacterial activity of P1 exhibited stability within the range of pH 4.5–6.5 and temperatures of 40–100 °C. The P1 exhibited relatively low hemolytic activity up to 8 mM. The P1 fraction at 8 mM suppressed the growth of <em>S. aureus</em> during a challenge test on commercial ultra-high temperature milk inoculated with <em>S. aureus</em> ATCC29213. Eleven novel hydrophilic peptides (6 cationic and 5 anionic) were identified and the peptide EAGGGEDDKKKVE showed the most potent antibacterial activity. We conclude that the pepsin-hydrolyzed CGM peptide fraction showed potential to be utilized as a novel antimicrobial agent for the control of <em>S. aureus</em> in foods.</div></div>","PeriodicalId":319,"journal":{"name":"Food Control","volume":"169 ","pages":"Article 110998"},"PeriodicalIF":5.6000,"publicationDate":"2024-11-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Control","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0956713524007151","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"FOOD SCIENCE & TECHNOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
The aim of this work was to determine the antibacterial properties and mode of activity of isolated corn gluten meal (CGM) hydrolysate fractions. The P1 fraction from reverse-phase liquid chromatography separation of pepsin-hydrolyzed CGM presented the most potent antibacterial activity with minimum inhibitory concentration (MIC) of 1 mM and 4 mM minimum bactericidal concentration (MBC) against Staphylococcus aureus ATCC29213. The kinetics of P1 antibacterial activity revealed a bacteriostatic effect at 1 × MIC and 2 × MIC for 8 h, but a bactericidal effect at 4 × MIC. The P1 fraction at 1 × MIC and 4 × MIC disrupted the membrane integrity of S. aureus after 8 h exposure as observed by confocal laser scanning microscopy. Scanning electron microscopy and transmission electron microscopy indicated cell surface damage and cytoplasmic leakage in S. aureus after being exposed to the P1 fraction. Synchrotron radiation-Fourier transmission infrared (SR-FTIR) microspectroscopy revealed changes in nucleic acid, protein, and fatty acid compositions of S. aureus cell membrane after 8 h exposure to P1 at 1 × MIC. The antibacterial activity of P1 exhibited stability within the range of pH 4.5–6.5 and temperatures of 40–100 °C. The P1 exhibited relatively low hemolytic activity up to 8 mM. The P1 fraction at 8 mM suppressed the growth of S. aureus during a challenge test on commercial ultra-high temperature milk inoculated with S. aureus ATCC29213. Eleven novel hydrophilic peptides (6 cationic and 5 anionic) were identified and the peptide EAGGGEDDKKKVE showed the most potent antibacterial activity. We conclude that the pepsin-hydrolyzed CGM peptide fraction showed potential to be utilized as a novel antimicrobial agent for the control of S. aureus in foods.
期刊介绍:
Food Control is an international journal that provides essential information for those involved in food safety and process control.
Food Control covers the below areas that relate to food process control or to food safety of human foods:
• Microbial food safety and antimicrobial systems
• Mycotoxins
• Hazard analysis, HACCP and food safety objectives
• Risk assessment, including microbial and chemical hazards
• Quality assurance
• Good manufacturing practices
• Food process systems design and control
• Food Packaging technology and materials in contact with foods
• Rapid methods of analysis and detection, including sensor technology
• Codes of practice, legislation and international harmonization
• Consumer issues
• Education, training and research needs.
The scope of Food Control is comprehensive and includes original research papers, authoritative reviews, short communications, comment articles that report on new developments in food control, and position papers.