Isolation, identification and characterization of a novel antimicrobial peptide from Moringa oleifera seeds based on affinity adsorption.
Isolation, identification and characterization of a novel antimicrobial peptide from Moringa oleifera seeds based on affinity adsorption.
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DOI：
10.1016/j.foodchem.2022.133923
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发表时间：
2022-08
期刊：
影响因子：
8.8
通讯作者：
Xuefeng Wang;Li He;Zhiyuan Huang;Qiong Zhao;J. Fan;Yang Tian;Aixiang Huang
中科院分区：
文献类型：
--
作者：
Xuefeng Wang;Li He;Zhiyuan Huang;Qiong Zhao;J. Fan;Yang Tian;Aixiang Huang
This study aimed to characterize a novel antimicrobial peptide (AMP) obtained fromMoringa oleiferaseed protein hydrolysates. Cell membrane chromatography and live bacteria adsorption were combined into a single step to efficiently isolate the active fraction of the AMP. Five peptides were identified by LC-MS/MS, among which the MCNDCGA peptide (termed MOp3) showed the greatest inhibitory effect against Staphylococcus aureus [minimum inhibitory concentration (MIC): 2 mg/mL]. MOp3 was identified as a hydrophobic anionic AMP rich in β-sheet structures with negligible hemolytic activity at 2.0 × MIC. MOp3 had good tolerance to salt solutions at 5 % and pH range 6.0–8.0, but was sensitive to high temperatures (>100 °C) and acid protease. Microscopic observation further revealed that MOp3 induced irreversible damage onto the cell membrane ofS. aureusand interacted with dihydrofolate reductase and DNA gyrase by hydrogen bonding and hydrophobic interaction. These findings highlight the potential application of a new antimicrobial agent againstS. aureusin the food industry.
