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Beyond Conventional Meat Preservation: Saddling the Control of Bacteriocin and Lactic Acid Bacteria for Clean Label and Functional Meat Products

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Abstract

Advancements in food science and technology have paved the way for the development of natural antimicrobial compounds to ensure the safety and quality of meat and meat products. Among these compounds, bacteriocin produced by lactic acid bacteria has gained considerable scientific attention for its ability to preserve the healthy properties of meat while preventing spoilage. This natural preservative is seen as a pioneering tool and a potent alternative to chemical preservatives and heat treatment, which can have harmful effects on the nutritional and sensory qualities of meat. Bacteriocin produced by lactic acid bacteria can be used in various forms, including as starter/protective cultures for fermented meats, purified or partially purified forms, loaded in active films/coatings, or established in encapsulate systems. This review delves into the downstream purification schemes of LAB bacteriocin, the elucidation of their characteristics, and their modes of action. Additionally, the application of LAB bacteriocins in meat and meat products is examined in detail. Overall, the use of LAB bacteriocins holds immense potential to inspire innovation in the meat industry, reducing the dependence on harmful chemical additives and minimizing the adverse effects of heat treatment on nutritional and sensory qualities. This review provides a comprehensive understanding of the potential of bacteriocin produced by lactic acid bacteria as a natural and effective meat preservative.

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Data Availability

Data will be made available on request.

Abbreviations

FAO:

Organization of the United Nations

LAB:

Lactic acid bacteria

GRAS:

Generally recognized as safe

Lan:

Lanthionine

MeLan:

β methyl lanthionine

Dha:

β unsaturated amino acids 2,3 didehydroalanine

Dhb:

2,3-didehydrobutyrine

RiPPs:

Ribosomally synthesized and post-translationally modified peptides

Ia:

lanthipeptides

Ib:

Head to tail cyclized peptides

LAP (Ic):

Linear azol(in)e containing peptides

Id:

Sactipeptides

Ie:

glycocins

If:

lasso peptides

man PTS:

Mannose phosphotransferase system

PPi:

Pyrophosphate

ATP:

Adenosine triphosphate

BLIS:

Bacteriocin-like inhibitory substance

WFH:

Wheat flour hydrolysate

MRS:

de Mann, Rogosa and Sharpe

PFM:

Proton motive force

UppP:

Undecaprenyl pyrophosphate phosphatase

HTP:

Huge toroidal pore

IEC:

Ion exchange chromatography

SEC:

Size exclusion chromatography

HIC:

Hydrophobic interaction chromatography

HPLC:

High-performance liquid chromatography

ATPS:

Aqueous two phase system

PEG:

Polyethylene glycol

MIC:

Minimum inhibitory concentration

PVDC:

Polyvinylidene chloride

LDPE:

Low density polyethylene

HDPE:

High density polyethylene

HPMC:

Hydroxypropyl methylcellulose

ACS:

Antimicrobial concentrated supernatant

CNFs:

Cellulose nanofibrils

PCL:

Poly(ε-caprolactone)

TBARS:

Thiobarbituric Acid Reactive Species

EDTA:

Ethylenediaminetetraacetic acid

PBAT/TPS:

Poly(butylene adipate terephthalate

HPP:

High Pressure Processing

LAE:

Lauric arginate

NCL:

Curcumin nanomats

TMAB:

Total mesophilic aerobic

ALG-GEL:

Alginate-gelatin

RTE:

Ready-to-Eat

PE:

Polyethylene

PP:

Polypropylene

MTGase:

Transglutaminase

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Authors and Affiliations

  1. Laboratory of Microbial, Enzymatic Biotechnology and Biomolecules (LBMEB), Center of Biotechnology of Sfax, University of Sfax, Road of Sidi Mansour Km 6, P.O. Box 1177, Sfax, 3018, Tunisia

    Slim Smaoui & Moufida Chaari

  2. Centro Tecnológico de la Carne de Galicia, Avd. Galicia nº 4, Parque Tecnológico de Galicia, Ourense, San Cibrao das Viñas, 32900, Spain

    Noemí Echegaray & Jose Manuel Lorenzo

  3. Chemical and Biochemical Processing Division, Central Institute for Research on Cotton Technology, Mumbai, 400019, India

    Manoj Kumar

  4. Deparment of Chemistry, Istituto Zooprofilattico Sperimentale della Puglia e della Basilicata, Via Manfredonia, 20, 71121, Foggia, Italy

    Teresa D’Amore

  5. Semey Branch of the Institute, Kazakh Research Institute of Processing and Food Industry, 238«G» Gagarin Ave, Almaty, 050060, Republic of Kazakhstan

    Mohammad Ali Shariati

  6. Department of Scientific Research, V. M. Gorbatov Federal Research Center for Food Systems of Russian Academy of Sciences, Moscow, 109316, Russian Federation

    Maksim Rebezov

  7. Área de Tecnología de los Alimentos, Facultad de Ciencias de Ourense, Universidade de Vigo, Ourense, 32004, Spain

    Jose Manuel Lorenzo

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  1. Slim Smaoui
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  2. Noemí Echegaray
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  3. Manoj Kumar
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  4. Moufida Chaari
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  6. Mohammad Ali Shariati
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  7. Maksim Rebezov
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  8. Jose Manuel Lorenzo
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Contributions

Conceptualization: S.S., M.A.S., and J.M.L; methodology: N.E.; software: T.D. and M.C.; validation: S.S. and J.M.L.; formal analysis: M.K; investigation: J.M.L.; resources: J.M.L.; data curation: S.S.; writing—original draft preparation: S.S., N.E., M.K., and T.D; writing—review and editing: S.S., M.A.S., M.R., and J.M.L; visualization: J.M.L.; supervision: J.M.L.; project administration: S.S. and J.M.L.; funding acquisition: J.M.L.

All authors have read and agreed to the published version of the manuscript.”

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Correspondence to Slim Smaoui or Mohammad Ali Shariati.

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Smaoui, S., Echegaray, N., Kumar, M. et al. Beyond Conventional Meat Preservation: Saddling the Control of Bacteriocin and Lactic Acid Bacteria for Clean Label and Functional Meat Products. Appl Biochem Biotechnol 196, 3604–3635 (2024). https://doi.org/10.1007/s12010-023-04680-x

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