Antimicrobial proteins are produced by bacteria (bacteriocins), frogs (magainins), insects (cecropins), and mammals (defensins). A common characteristic among these agents is their proteinaceous composition and antimicrobial activity. In spite of distinct differences in genetic organization (eukaryotic vs. prokaryotic) of these inhibitory agents, there are definite similarities in biological activity which relates to their molecular structure. The lactic acid bacteria (LAB), long known for their acidifying properties and applications in food fermentations, are now becoming widely recognized for the production of bacteriocins. The widespread application of LAB in cultured/fermented foods, their recognition as safe "food-grade" organisms, and their presence as part of the human intestinal flora has facilitated the application of their bacteriocins as antimicrobial agents in food. LAB bacteriocins would likely be more acceptable than antimicrobial peptides from other sources, however, they are mainly effective against Gram-positive organisms. Eukaryotic antimicrobial peptides are unique in that they are also inhibitory towards Gram-negative bacteria, fungi, and protozoa. Information on antimicrobial peptides from various sources may provide a greater understanding of their mode of action and facilitate their application as "biopreservatives" in food.
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