Proteolytic-derived antimicrobial peptides from Lactiplantibacillus plantarum: From mechanism to application in fermented foods.

The demand for natural preservatives has increased interests in antimicrobial peptides (AMPs) from Lactiplantibacillus plantarum. Beyond ribosomal bacteriocins, its proteolytic system generates AMPs from food proteins, with activities ranging from low μg mL-1 (purified peptides) to mg mL-1 (crude hydrolysates). In this process, cell-envelope proteinases initiate protein cleavage, Opp/DtpT systems transport peptides, and intracellular peptidases produce active AMPs. These amphipathic, hydrophobic and basic residue-rich peptides primarily form membrane pores or target the mannose phosphotransferase receptor. Applications in fermented foods show promise for biopreservation, shelf-life extension, texture improvement, and nitrite reduction. However, industrial translation is limited by yield variability, matrix interference, high purification costs, and the need for strain-specific safety evaluation. Future advances require an integrated strategy combining omics, CRISPR-based metabolic engineering, and microencapsulation to optimize yield, stability, and delivery. This review provides a roadmap for engineering L. plantarum as a natural bio-preservative factory for safer, clean-label fermented foods.