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Updated: Jun 12, 2025
Author Spotlight: Integrating Biochemical Functions of β-Glucanases and Peroxidase Enzymes in Wheat-RWA Interaction
Published on: July 26, 2024
A novel antimicrobial peptide WBp-1 from wheat bran: Purification, characterization and antibacterial potential
Zhipeng Zou1, Michelle A Purnawan1, Yiming Wang1
1College of Biosystems Engineering and Food Science, National-Local Joint Engineering Laboratory of Intelligent Food Technology and Equipment, Zhejiang Key Laboratory for Agro-Food Processing, Integrated Research Base of Southern Fruit and Vegetable Preservation Technology, Zhejiang International Scientific and Technological Cooperation Base of Health Food Manufacturing and Quality Control, Zhejiang University, Hangzhou 310058, China.
Abstract:
This study introduces a novel antimicrobial peptide (AMP), WBp-1, isolated from wheat bran and purified via reversed-phase high-performance liquid chromatography. The amino acid sequence, determined as IITGASSGIGKAIAKHFI by LC-MS/MS, was composed predominantly of alkaline and hydrophobic residues. WBp-1 was predicted to be a stable, hydrophobic, cationic peptide with an α-helical structure. Moreover, it displayed significant antibacterial efficacy against Listeria monocytogenes, with a minimum inhibitory concentration of 150 μg/mL. Further mechanistic studies suggest that WBp-1 exerts its bactericidal activity by disrupting cell membrane integrity, impeding peptidoglycan synthesis by binding to penicillin-binding protein 4 via hydrogen bonding, increasing cell permeability, altering membrane potential and fluidity, and altering surface hydrophobicity. Interestingly, WBp-1 showed minimal hemolytic activity and cytotoxicity against LO2 cells, even at 16× MIC. These findings highlight the strong potential of WBp-1 as a novel antibacterial agent and food preservative against Listeria monocytogenes.
