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Review
. 2024 Oct 17;13(4):12558.
doi: 10.4081/ijfs.2024.12558. eCollection 2024 Nov 12.

Biopreservation strategies using bacteriocins to control meat spoilage and foodborne outbreaks

Affiliations
Review

Biopreservation strategies using bacteriocins to control meat spoilage and foodborne outbreaks

Nathália Fernandes et al. Ital J Food Saf. .

Abstract

Fresh meat is highly perishable, presenting challenges in spoilage mitigation and waste reduction globally. Despite the efforts, foodborne outbreaks from meat consumption persist. Biopreservation offers a natural solution to extend shelf life by managing microbial communities. However, challenges include the effective diffusion of bacteriocins through the meat matrix and the potential inhibition of starter cultures by bacteriocins targeting closely related lactic acid bacteria (LAB). LAB, predominant in meat, produce bacteriocins - small, stable peptides with broad antimicrobial properties effective across varying pH and temperature conditions. This review highlights the recent advances in the optimization of bacteriocin use, considering its structure and mode of action. Moreover, the strengths and weaknesses of different techniques for bacteriocin screening, including novel bioengineering methods, are described. Finally, we discuss the advantages and limitations of the modes of application of bacteriocins toward the preservation of fresh, cured, and novel meat products.

Keywords: antimicrobial peptides; biopreservation; lactic acid bacteria; meat.

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Conflict of interest statement

Conflict of interest: the authors declare no conflict of interest.

Figures

Figure 1.
Figure 1.
Nisin mode of action.
Figure 2.
Figure 2.
Pediocin-PA-1 mode of action.
Figure 3.
Figure 3.
Diagram for different in vitro methods for bacteriocin activity screening from foodstuffs.
Figure 4.
Figure 4.
The amino acid composition of nisin.
Figure 5.
Figure 5.
Lantibiotics three-dimensional primary structures. A) Nisin A (P13068); B) nisin Z (P29559); C) lactocin S (P23826).
Figure 6.
Figure 6.
Representation of class IIa bacteriocins isolated from meat aligned by the CLUSTAL W algorithm and visualized in Jalview.
Figure 7.
Figure 7.
3D primary structures of class IIa bacteriocins. A) Pediocin PA-1 (P29430); B) divergicin 750 (Q46597); C) carnobacteriocin A (P38578).
Figure 8.
Figure 8.
Diagram of lactic acid bacteria biofilm and bacteriocin for different kinds of applications in the processing and conservation of meat and meat products.

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