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Review
. 2023 Mar 17;12(3):477.
doi: 10.3390/pathogens12030477.

Bioactive Antimicrobial Peptides from Food Proteins: Perspectives and Challenges for Controlling Foodborne Pathogens

Affiliations
Review

Bioactive Antimicrobial Peptides from Food Proteins: Perspectives and Challenges for Controlling Foodborne Pathogens

Jessica Audrey Feijó Corrêa et al. Pathogens. .

Abstract

Bioactive peptides (BAPs) derived from food proteins have been extensively studied for their health benefits, majorly exploring their potential use as nutraceuticals and functional food components. These peptides possess a range of beneficial properties, including antihypertensive, antioxidant, immunomodulatory, and antibacterial activities, and are naturally present within dietary protein sequences. To release food-grade antimicrobial peptides (AMPs), enzymatic protein hydrolysis or microbial fermentation, such as with lactic acid bacteria (LAB), can be employed. The activity of AMPs is influenced by various structural characteristics, including the amino acid composition, three-dimensional conformation, liquid charge, putative domains, and resulting hydrophobicity. This review discusses the synthesis of BAPs and AMPs, their potential for controlling foodborne pathogens, their mechanisms of action, and the challenges and prospects faced by the food industry. BAPs can regulate gut microbiota by promoting the growth of beneficial bacteria or by directly inhibiting pathogenic microorganisms. LAB-promoted hydrolysis of dietary proteins occurs naturally in both the matrix and the gastrointestinal tract. However, several obstacles must be overcome before BAPs can replace antimicrobials in food production. These include the high manufacturing costs of current technologies, limited in vivo and matrix data, and the difficulties associated with standardization and commercial-scale production.

Keywords: antimicrobial peptides; encrypted peptides; lactic acid bacteria; protein-rich by-products; whey protein.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Schematic representation of the generation of BAPs. A generic globular protein is hydrolyzed, releasing the encrypted peptides from the protein matrix. Some of the released peptides may present interesting bioactivities, such as antimicrobial effects towards foodborne pathogens—the focus of this review.

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