Use of Lactoperoxidase Inhibitory Effects to Extend the Shelf Life of Meat and Meat Products

. 2024 May 17 ; 12 (5) : . [epub] 20240517

Status PubMed-not-MEDLINE Jazyk angličtina Země Švýcarsko Médium electronic

Typ dokumentu časopisecké články

Perzistentní odkaz   https://www.medvik.cz/link/pmid38792839

Grantová podpora
This work was supported from the grant of Specific university research - grant No A1_FPBT_2024_008 University of Chemistry and Technology, Prague

Odkazy

PubMed 38792839
PubMed Central PMC11124385
DOI 10.3390/microorganisms12051010
PII: microorganisms12051010
Knihovny.cz E-zdroje

Lactoperoxidase (LP) is an important enzyme of the salivary and mammary glands. It has been proven to increase the shelf life of raw milk by inhibiting the growth of bacteria, especially Listeria monocytogenes, Escherichia coli, Staphylococcus aureus, and Pseudomonas spp. The aim of this work was to verify the use of LP to extend the shelf life of meat products. In vitro experiments showed inhibitory effects on the selected bacteria (Listeria innocua (ATCC 33090), Staphylococcus saprophyticus (CP054440.1), and Pseudomonas fluorescens (ATCC 13525) due to a prolongation of the lag phase of growth curves. A lower increase in viable counts (p < 0.05) was also found by testing pork cubes' surface treated with LP solution (5%) + L. innocua and stored for 7 days at 15 °C. LP has also been studied at concentrations of 0.25 and 0.50% in meat products (pork ham and pâté) during refrigerated storage (4 °C for 28 days). Lower viable counts were observed throughout the storage experiment, especially for 0.50% LP (p < 0.05). Meat products containing LP also showed lower levels of oxidation (MAD) (p < 0.05). According to these results, LP could extend the shelf life of a wider range of products.

Zobrazit více v PubMed

Kennedy M., O’Rourke A.-L., McLay J., Simmonds R. Use of a ground beef model to assess the effect of the lactoperoxidase system on the growth of Escherichia coli O157:H7, Listeria monocytogenes and Staphylococcus aureus in red meat. Int. J. Food Microbiol. 2000;57:147–158. doi: 10.1016/S0168-1605(99)00208-1. PubMed DOI

Kaur R., Kaur L., Gupta T.B., Singh J., Bronlund J. Multitarget preservation technologies for chemical-free sustainable meat processing. J. Food Sci. 2022;87:4312–4328. doi: 10.1111/1750-3841.16329. PubMed DOI PMC

Crowe W., Elliot C.T., Green B.D. A Review of the In Vivo Evidence Investigating the Role of Nitrite Exposure from Processed Meat Consumption in the Development of Colorectal Cancer. Nutrients. 2019;11:2673. doi: 10.3390/nu11112673. PubMed DOI PMC

Tenovuo J., Pruitt K.M. Relationship of the human salivary peroxidase system to oral health. J. Oral Pathol. 1984;13:573–584. doi: 10.1111/j.1600-0714.1984.tb01459.x. PubMed DOI

Sharma S., Singh A.K., Kaushik S., Sinha M., Singh R.P., Sharma P., Sirohi H., Kaur P., Singh T.P. Lactoperoxidase: Structural insights into the function, ligand binding and inhibition. Int. J. Biochem. Mol. Biol. 2013;13:108–128. PubMed PMC

Hoogendoorn H., Piessens J.P., Scholtes W., Stoddard L.A. Hypothiocyanite ion; the inhibitor formed by the system lactoperoxidase-thiocyanate-hydrogen peroxide. I. Identification of the inhibiting compound. Caries Res. 1977;11:77–84. doi: 10.1159/000260252. PubMed DOI

Seifu E., Buys E.M., Donkin E.F. Significance of lactoperoxidase system in the dairy industry and its potential applications: A review. Trends Food Sci. Technol. 2005;16:137–154. doi: 10.1016/j.tifs.2004.11.002. DOI

Reiter B., Härnulv G. Lactoperoxidase Antibacterial System: Natural Occurrence, Biological Functions and Practical Applications. J. Food Prot. 1984;47:724–732. doi: 10.4315/0362-028X-47.9.724. PubMed DOI

Elliot R.M., McLay J.C., Kennedy M.J., Simmonds R.S. Inhibition of foodborne bacteria by the lactoperoxidase system in a beef cube system. Int. J. Food Microbiol. 2004;91:73–81. doi: 10.1016/S0168-1605(03)00366-0. PubMed DOI

Al-Baarri A.N., Damayanti N.T., Legowo A.M., Tekiner İ.H. Enhanced Antibacterial Activity of Lactoperoxidase–Thiocyanate–Hydrogen Peroxide System in Reduced-Lactose Milk Whey. Int. J. Food Sci. 2019;2019:8013402. doi: 10.1155/2019/8013402. PubMed DOI PMC

Bafort F., Parisi O., Perraudin J.P., Jijakli M.H. Mode of action of lactoperoxidase as related to its antimicrobial activity: A review. Enzym. Res. 2014;2014:517164. doi: 10.1155/2014/517164. PubMed DOI PMC

Al-Baarri A.N., Ogawa M., Hayakawa S. Scale-up studies on immobilisation of lactoperoxidase using milk whey for producing antimicrobial agent. J. Indones. Trop. Anim. Agric. 2010;35:185–191. doi: 10.14710/jitaa.35.3.185-191. DOI

Whitaker J.R., Voragen A.G.J., Wonf D.W.S. Handbook of Food Enzymology. CRP Press; Marcel Dekker, NY, USA: 2003. pp. 263–286.

Almehdar H.A., El-Fakharany E.M., Uversky V.N., Redwan E.M. Disorder in milk proteins: Structure, functional disorder, and biocidal potentials of lactoperoxidase. Curr. Protein Pept. Sci. 2015;16:352–365. doi: 10.2174/1389203716666150316114956. PubMed DOI

Sousa S.G., Delgadillo I., Saraiva J.A. Effect of thermal pasteurisation and high-pressure processing on immunoglobulin content and lysozyme and lactoperoxidase activity in human colostrum. Food Chem. 2014;151:79–85. doi: 10.1016/j.foodchem.2013.11.024. PubMed DOI

Silva E., Oliveira J., Silva Y., Urbano S., Sales D., Moraes E., Rangel A., Anaya K. Lactoperoxidase system in the dairy industry: Challenges and opportunities. Czech J. Food Sci. 2020;38:337–346. doi: 10.17221/103/2020-CJFS. DOI

Magacz M., Kędziora K., Sapa J., Krzyściak W. The Significance of Lactoperoxidase System in Oral Health: Application and Efficacy in Oral Hygiene Products. Int. J. Mol. Sci. 2019;20:1443. doi: 10.3390/ijms20061443. PubMed DOI PMC

de Wit J.N., van Hooydonk A.C.M. Structure, functions and applications of lactoperoxidase in natural antimicrobial systems. Neth. Milk Dairy J. 1996;50:227–244.

Wolfson L.M., Sumner S.S. Antibacterial activity of the lactoperoxidase system: A review. J. Food Prot. 1993;56:887–892. doi: 10.4315/0362-028X-56.10.887. PubMed DOI

Korhonen H. A new method for preserving raw milk—The lactoperoxidase antibacterial system. World Anim. Rev. 1980;35:23–29.

Marks N.E., Grandison A.S., Lewis M.J. Challenge testing of the lactoperoxidase system in pasteurised skim milk. J. Appl. Microbiol. 2001;91:735–741. doi: 10.1046/j.1365-2672.2001.01435.x. PubMed DOI

Dumitrascu L., Stanciuc N., Stanciu S., Râpeanu G. Thermal inactivation of lactoperoxidase in goat, sheep and bovine milk—A comparative kinetic and thermodynamic study. J. Food Eng. 2012;113:47–52. doi: 10.1016/j.jfoodeng.2012.05.028. DOI

Czech Republic: Decree on Requirements for Meat, Meat Product, Fishery and Aquaculture Products and Products Thereof, Eggs and Products Thereof. Collection of laws Czech Republic; Brno, Czech Republic: 2016. Decree No. 69/2016 Coll; pp. 714–759.

Beňo F., Horsáková I., Kmoch M., Petrzik K., Krátká G., Ševčík R. Bacteriophages as a Strategy to Protect Potato Tubers against Dickeya dianthicola and Pectobacterium carotovorum Soft Rot. Microorganisms. 2022;10:2369. doi: 10.3390/microorganisms10122369. PubMed DOI PMC

Kaczmarek A., Cegielska-Radziejewska R., Szablewski T., Zabielski J. TBARS and Microbial Growth Predicative Models of Pork Sausage Stored at Different Temperatures. Czech J. Food Sci. 2015;96:320–325. doi: 10.17221/591/2014-CJFS. DOI

Yu H.H., Chin Y.-W., Paik H.-D. Application of Natural Preservatives for Meat and Meat Products against Food-Borne Pathogens and Spoilage Bacteria: A Review. Foods. 2021;10:2418. doi: 10.3390/foods10102418. PubMed DOI PMC

Jooyandeh H., Aberoumand A., Nasehi B. Application of lactoperoxidase system in fish and food products: A review. Am. Eurasian J. Agric. Environ. Sci. 2011;10:89–96.

Aprodu J., Stanciuc N., Dumitrascu L., Râpeanu G., Stanciu S. Investigations towards understanding the thermal denaturation of lactoperoxidase. Inter. Dairy J. 2014;38:47–54. doi: 10.1016/j.idairyj.2014.03.013. DOI

Lara-Aguilar S., Alcaine D.S. Lactose oxidase: A novel activator of the lactoperoxidase system in milk for improved shelf life. J. Dairy Sci. 2019;102:1933–1942. doi: 10.3168/jds.2018-15537. PubMed DOI

Min S., Harris L.J., Krochta J.M. Inhibition of Salmonella enterica and Escherichia coli O157: H7 on roasted turkey by edible whey protein coatings incorporating the lactoperoxidase system. J. Food Prot. 2006;69:784–793. doi: 10.4315/0362-028X-69.4.784. PubMed DOI

Ehsani A., Hashemi M., Afshari A., Aminzare M., Raeisi M., Tayeheb Z. Effect of different types of active biodegradable films containing lactoperoxidase system or sage essential oil on the shelf life of fish burger during refrigerated storage. LWT. 2020;117:108633. doi: 10.1016/j.lwt.2019.108633. DOI

Bensid A., Ucar Y., Bendeddouche B., Özogul F. Effect of the icing with thyme, oregano and clove extracts on quality parameters of gutted and beheaded anchovy (Engraulis encrasicholus) during chilled storage. Food Chem. 2014;145:681–686. doi: 10.1016/j.foodchem.2013.08.106. PubMed DOI

Farshidi M., Yousefi M., Ehsani A. The combined effects of lactoperoxidase system and whey protein coating on microbial, chemical, textural, and sensory quality of shrimp (Penaeus merguiensis) during cold storage (4 ± 1 °C) Food Sci. Nutr. 2018;6:1378–1386. doi: 10.1002/fsn3.669. PubMed DOI PMC

Shokri S., Ehsani A., Jasour M.S. Efficacy of lactoperoxidase system-whey protein coating on shelf-life extension of rainbow trout fillets during cold storage (4 °C) Food Bioprocess Technol. 2015;8:54–62. doi: 10.1007/s11947-014-1378-7. DOI

Rostami H., Abbaszadeh S., Shokri S. Combined effects of lactoperoxidase system-whey protein coating and modified atmosphere packaging on the microbiological, chemical and sensory attributes of Pike-Perch fillets. J. Food Sci. Technol. 2017;54:3243–3250. doi: 10.1007/s13197-017-2767-5. PubMed DOI PMC

Jasour M.S., Ehsani A., Mehryar L., Naghibi S.S. Chitosan coating incorporated with the lactoperoxidase system: An active edible coating for fish preservation. J. Sci. Food Agric. 2015;95:1373–1378. doi: 10.1002/jsfa.6838. PubMed DOI

Dimova M., Tugai A., Tugai T., Iutynska G., Dordevic D., Kushkevych I. Molecular Research of Lipid Peroxidation and Antioxidant Enzyme Activity of Comamonas testosteroni Bacterial Cells under the Hexachlorobenzene Impact. Int. J. Mol. Sci. 2022;23:11415. doi: 10.3390/ijms231911415. PubMed DOI PMC

Gęgotek A., Skrzydlewska E. Biological Effect of Protein Modifications by Lipid Peroxidation Products. Chem. Phys. Lipids. 2019;221:46–52. doi: 10.1016/j.chemphyslip.2019.03.011. PubMed DOI

Najít záznam

Citační ukazatele

Nahrávání dat ...

Možnosti archivace

Nahrávání dat ...