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Enzyme Research
Volume 2014, Article ID 517164, 13 pages
Review Article

Mode of Action of Lactoperoxidase as Related to Its Antimicrobial Activity: A Review

1Plant Pathology Laboratory, Liége University, Gembloux Agro-Bio Tech, Passage des Déportés 2, 5030 Gembloux, Belgium
2Taradon Laboratory, Avenue Léon Champagne 2, 1480 Tubize, Belgium

Received 17 June 2014; Revised 19 August 2014; Accepted 19 August 2014; Published 16 September 2014

Academic Editor: Qi-Zhuang Ye

Copyright © 2014 F. Bafort et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Lactoperoxidase is a member of the family of the mammalian heme peroxidases which have a broad spectrum of activity. Their best known effect is their antimicrobial activity that arouses much interest in in vivo and in vitro applications. In this context, the proper use of lactoperoxidase needs a good understanding of its mode of action, of the factors that favor or limit its activity, and of the features and properties of the active molecules. The first part of this review describes briefly the classification of mammalian peroxidases and their role in the human immune system and in host cell damage. The second part summarizes present knowledge on the mode of action of lactoperoxidase, with special focus on the characteristics to be taken into account for in vitro or in vivo antimicrobial use. The last part looks upon the characteristics of the active molecule produced by lactoperoxidase in the presence of thiocyanate and/or iodide with implication(s) on its antimicrobial activity.