Lactoperoxidase: Properties, Functions and Potential Applications

Lactoperoxidase (LPO) (E.C. 1.11.1.7) is a member of the superfamily of mammalian heme peroxidases that is isolated from milk, and it is the first enzyme announced to be found in milk. LPO is found in milk, saliva, tears, and airways. It contributes significantly to the self-defense of the mammal body. It catalyzes oxidation of certain molecules such as thiocyanate (SCN⁻), I⁻ and Br⁻ in the presence of hydrogen peroxide (H2O2). Therefore, it produces new molecules that have a great antimicrobial spectrum, including antibacte-rial, antiviral, and antifungal activity, especially thiocyanate (SCN⁻) and hypoiodite (OI⁻), which are coming into prominence via their high antimicrobial activity. The lactop-eroxidase system (LPOS) is the system consisting of LPO, H2O2 and SCN⁻. LPO has a great potential to be used in various areas such as preservation and shelf-life elongation of milk, milk products, meat, meat products, plants including fruits and vegetables, and oral care, diagnosis, immunomodulation, and treatment of nephrotoxicity. The LPO gene, along with LPO itself, is important for animals. In the absence of the LPO gene, an increase in the frequency of diverse diseases including inflammation, tumor formation, and obesity. In this review, we mentioned general information about the enzyme LPO and its po-tential. Chemical properties and other features of other components of LPOS, H2O2 and SCN⁻, were also touched on the review. Lastly, we discussed potential applications of LPO in different areas and left future remarks, in the light of recent studies.