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Review
. 2019 Mar 21;20(6):1443.
doi: 10.3390/ijms20061443.

The Significance of Lactoperoxidase System in Oral Health: Application and Efficacy in Oral Hygiene Products

Marcin Magacz  1 , Karolina Kędziora  2 , Jacek Sapa  3 , Wirginia Krzyściak  4
Affiliations
Review

The Significance of Lactoperoxidase System in Oral Health: Application and Efficacy in Oral Hygiene Products

Marcin Magacz et al. Int J Mol Sci. .

Abstract

Lactoperoxidase (LPO) present in saliva are an important element of the nonspecific immune response involved in maintaining oral health. The main role of this enzyme is to oxidize salivary thiocyanate ions (SCN-) in the presence of hydrogen peroxide (H₂O₂) to products that exhibit antimicrobial activity. LPO derived from bovine milk has found an application in food, cosmetics, and medical industries due to its structural and functional similarity to the human enzyme. Oral hygiene products enriched with the LPO system constitute an alternative to the classic fluoride caries prophylaxis. This review describes the physiological role of human salivary lactoperoxidase and compares the results of clinical trials and in vitro studies of LPO alone and complex dentifrices enriched with bovine LPO. The role of reactivators and inhibitors of LPO is discussed together with the possibility of using nanoparticles to increase the stabilization and activity of this enzyme.

Keywords: caries prophylaxis; dentifrice; lactoperoxidase; periodontitis prophylaxis; saliva.

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Conflict of interest statement

The authors declare no conflicts of interest.

Figures

Figure 1
Figure 1
Activity of lactoperoxidase (LPO) in human milk and colostrum [35], milk of cows [64], buffalos [65], goats [66], sheep [67], and guinea pigs [69]. Comparison of LPO activity studies conducted by different teams may be problematic and subject to error due to the lack of standardization of the conditions of the analysis and the applied unit of activity.
See this image and copyright information in PMC

References

    1. Ihalin R., Loimaranta V., Tenovuo J. Origin, structure, and biological activities of peroxidases in human saliva. Arch. Biochem. Biophys. 2006;445:261–268. doi: 10.1016/j.abb.2005.07.004. - DOI - PubMed
    1. 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;2014:1–13. doi: 10.1155/2014/517164. - DOI - PMC - PubMed
    1. Gudipaneni R.K., Kumar R.V., Jesudass G., Peddengatagari S., Duddu Y. Short term comparative evaluation of antimicrobial efficacy of tooth paste containing lactoferrin, lysozyme, lactoperoxidase in children with severe early childhood caries: A clinical study. J. Clin. Diagn. Res. 2014;8:ZC18–ZC20. doi: 10.7860/JCDR/2014/8161.4232. - DOI - PMC - PubMed
    1. Shimizu E., Kobayashi T., Wakabayashi H., Yamauchi K., Iwatsuki K., Yoshie H. Effects of Orally Administered Lactoferrin and Lactoperoxidase-Containing Tablets on Clinical and Bacteriological Profiles in Chronic Periodontitis Patients. Int. J. Dent. 2011;2011:1–9. doi: 10.1155/2011/405139. - DOI - PMC - PubMed
    1. Borzouee F., Mofid M.R., Varshosaz J., Samsam Shariat S.Z.A. Purification of lactoperoxidase from bovine whey and investigation of kinetic parameters. Adv. Biomed. Res. 2016;5:189. - PMC - PubMed

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