Lactoperoxidase and thiocyanate were shown to protect Escherichia coli and three oral streptococcal species from the bactericidal effect of hydrogen peroxide under aerobic conditions. Lactoperoxidase in the absence of thiocyanate was also protective for two of the bacterial species in a dilution medium but potentiated hydrogen peroxide toxicity for the other two under the same conditions. The p...

We have studied inactivation of four strains each of Escherichia coli and Listeria innocua in milk by the combined use of high hydrostatic pressure and the lactoperoxidase-thiocyanate-hydrogen peroxide system as a potential mild food preservation method. The lactoperoxidase system alone exerted a bacteriostatic effect on both species for at least 24 h at room temperature, but none of the strain...

The enzyme lactoperoxidase is part of the innate immune system in vertebrates and owes its antimicrobial activity to the formation of oxidative reaction products from various substrates. In a previous study, we have reported that, with thiocyanate as a substrate, the lactoperoxidase system elicits a distinct stress response in Escherichia coli MG1655. This response is different from but partly ...

1. The products of the lactoperoxidase-catalysed oxidation of thiocyanate by hydrogen peroxide were sulphate, carbon dioxide and ammonia. Cyanate, sulphite and a compound showing increased extinction at 235mmu (the ;235 compound') were intermediate oxidation products. 2. Two of the intermediates acted as electron acceptors in the oxidation of NADH(2). Thus NADH(2) was oxidized by sulphite in th...

1. The products of the lactoperoxidase-catalysed oxidation of thiocyanate by hydrogen peroxide were sulphate, carbon dioxide and ammonia. Cyanate, sulphite and a compound showing increased extinction at 235m,u (the '235 compound') were intermediate oxidation products. 2. Two of the intermediates acted as electron acceptors in the oxidation of NADH2. Thus NADH2 was oxidized by sulphite in the pr...

Background The heme enzyme lactoperoxidase is found in body secretions where it significantly contributes to the humoral immune response against pathogens. After activation the peroxidase oxidizes thiocyanate to hypothiocyanite which is known for its microbicidal properties. Yet several pathologies are accompanied by a disturbed hypothiocyanite production which results in a reduced immune defen...

Sindbis virus was iodinated by using the enzyme lactoperoxidase, an iodination technique which labels only surface proteins. By this technique, the two viral glycoproteins are labeled, and the internal viral protein is not. The two glycoproteins are iodinated to strikingly different extents. This difference in susceptibility to iodination apparently is due to the position or conformation of the...

background: lactoperoxidase (lpo) is one of the most heat-stable enzymes in milk and its inactivation has been proposed for monitoring thermal processes. the aim of this study was to provide information on activity and thermal inactivation behavior of lpo in iranian cow and buffalo milk and whey. methods: sixty cow and buffalo milk samples were collected. the lpo activity was measured using spe...