This study developed antimicrobial peptides (AMPs) from quinoa with high antibacterial activity and stability by mixed-bacteria fermentation. Furthermore, among 9 peptide fractions purified by membrane separation and chromatography, F1 could effectively inhibit the growth and propagation of bacterial microorganisms in apple juice. Subsequently, F1 identified LC-MS/MS as 95 peptides, molecular weights 494.25 Da to 1253.55 Da, notably, AGAAPE peptide (556.25 Da), negatively charged (-1), highly hydrophobic (50 %), with significant inhibitory effects on both Escherichia coli and Staphylococcus aureus (MIC 5 mg/mL). The antimicrobial mechanism of AGAAPE was determined to damage membrane through hydrogen-bond and hydrophobic interactions, resulting in leakage of intramembrane substances and inhibition of intracellular ATPase activity. Moreover, AGAAPE was pH resistant (pH 4-12), thermally stable (121 °C, 30 min), resistant to salt ion interference (Na, Ca), and protease hydrolysis resistant (neutral protease, pepsin, trypsin). Overall, identifying AMPs from quinoa provides a promising new approach for fresh juice preservation.
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http://dx.doi.org/10.1016/j.foodchem.2024.142536 | DOI Listing |
Food Chem
December 2024
Xinjiang Key Laboratory of Biological Resources and Genetic Engineering, College of Life Science and Technology, Xinjiang University, Urumqi 830017, China. Electronic address:
This study developed antimicrobial peptides (AMPs) from quinoa with high antibacterial activity and stability by mixed-bacteria fermentation. Furthermore, among 9 peptide fractions purified by membrane separation and chromatography, F1 could effectively inhibit the growth and propagation of bacterial microorganisms in apple juice. Subsequently, F1 identified LC-MS/MS as 95 peptides, molecular weights 494.
View Article and Find Full Text PDFVestn Otorinolaringol
December 2024
Sverzhevsky Research Clinical Institute of Otorhinolaryngology, Moscow, Russia.
Otitis externa is one of the most common diseases in otorhinolaryngological practice frequently requiring prescription of analgesic medications and antimicrobials. The total of 2714 patients were included in the retrospective study to evaluate bacterial etiology, effectiveness, and safety of topical empirical treatment of patients with diagnosed otitis externa during 2018-2023. The most common pathogens isolated were (38.
View Article and Find Full Text PDFJ Agric Food Chem
December 2024
MOE Key Laboratory of Bio-Intelligent Manufacturing, School of Bioengineering, Dalian University of Technology, Dalian 116024, China.
Plant natural products are crucial in defending against herbivorous insects and are widely used in pest control, yet their mechanisms remain complex and insufficiently studied. This study employed a reverse strategy to investigate the mechanism of camptothecin (CPT), a botanical pesticide. By using a CPT-based chemical probe coupled with proteomic analysis, immune-related proteins, including those involved in prophenoloxidase (PPO) activation and antimicrobial peptide (AMP) synthesis, were identified in the Asian corn borer, .
View Article and Find Full Text PDFJ Fungi (Basel)
December 2024
School of Biological Engineering, Sichuan University of Science & Engineering, Yibin 644000, China.
This study examined the efficacy and mechanisms of action of the antimicrobial peptide BP15 and its lipopeptides, HBP15 and LBP15, against , the primary causative agent of green mold in citrus fruits. The findings revealed that all three antimicrobial peptides markedly inhibited the spore germination and mycelial growth of , with minimum inhibitory concentrations (MICs) of 3.12 μM for BP15, HBP15, and LBP15.
View Article and Find Full Text PDFMar Drugs
November 2024
Guangxi Key Laboratory of Beibu Gulf Marine Biodiversity Conservation, Beibu Gulf University, Qinzhou 535011, China.
Crustins are a family of antimicrobial peptides (AMPs) that play a pivotal role in the innate immune system of crustaceans. The discovery of novel AMPs from natural sources is crucial for expanding our current database of these peptides. Here, we identified and characterized a novel member of the crustin family, named Crus-SWD1, derived from .
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