Lactoperoxidase (LPO) is one of the crucial enzymes in milk with oxidoreductase activity. The peroxidase isolated from milk was given the name lactoperoxidase and was the first enzyme reported to be found in milk. The main function of the enzyme is to catalyze the oxidation of molecules in the presence of hydrogen peroxide and to help the production of products with a wide antimicrobial activity.
The lactoperoxidase is also one of the sources of Lactoperoxidase. Pseudohalogens, thiocyanates, or halogens should function as second substrates for the enzyme to exhibit such antimicrobial effects.
There are several ways in which the spoilage of milk may be controlled, including refrigeration, heat treatment (pasteurization in bulk or pouch), microfiltration (with or without pasteurization), bactofugation, high-pressure treatment and use of chemical preservatives (including salting at levels of 3–12%). Some of these procedures require expensive equipment and are not widely applicable, particularly in small-scale dairy production and processing systems in developing countries where up to 80% of the milk produced may enter the informal market.
Is lactoperoxidase supplement effective?
The effectiveness of the LP-s in maintaining the hygienic quality of raw milk for a limited period has been established in many experimental and field studies conducted in different geographical regions. The method can be applied to preserve raw milk from different species. The effectiveness depends on the initial amount and type of microbiological contamination and the temperature of milk during the treatment period. The LP-s exerts primarily a bacteriostatic effect in raw milk.
Both pure LPO preparations and other microbiologically reactive components such as lactoperoxidase supplement or immunoglobulins are used in the production of oral hygiene preparations [70,71]. Some methods have been developed for obtaining clean preparations of LPO and lactoferrin in one process .
How many stages of processing and Purification takes place?
LPO purification procedures on both industrial and laboratory scales cover many stages and are time-consuming. Before the application of specific cleaning techniques, certain processes are used to densify the material and eliminate the main undesirable substances. These processes include fat centrifugation, removal of casein by adding rennet, removal of unnecessary major milk protein fractions, and concentration by precipitation with ammonium sulfate [5,64]. The use of affinity chromatography allows us to obtain very pure LPO preparations (e.g., purification fold 3397, 7.6% yield
The issue of whether long-term use of the LP-s would result in any microbiological risks, e.g. development of LP-s resistant, antibiotic-resistant or toxin-producing bacteria was considered.
The LPO system shows a significant protective effect in bovine milk. The activation of the system depends on the concentration of the two reactants, thiocyanate and hydrogen peroxide. In the presence of hydrogen peroxide, the system catalyzes the transformation of thiocyanate into hypothiocyanate, which has an antibacterial nature. The end products of these compounds are oxidized and hence are safe for human health.
The LP-s elicits antimicrobial activity against a wide variety of milk spoilage and pathogenic microorganisms including bacteria, viruses, molds, yeasts, mycoplasma, and protozoa. The overall activity is primarily bacteriostatic3 or igg powder buy, depending on the initial total bacterial load, species and strains of contaminating bacteria and the temperature of the milk. While its effectiveness against well-known milk spoilage and pathogenic microorganisms is well established, further studies would be useful on the efficacy of the LP-s against milk-borne viruses and emerging pathogenic microorganisms.