Ex vivo decontamination of yeast-colonized dentures by iodine-thiocyanate complexes.

Introduction: Under well-defined experimental conditions, and in the presence of hydrogen peroxide, lactoperoxidase produces stable iodine-thiocyanate complexes that have antimicrobial properties. A novel process was developed to short circuit the consumption of hydrogen peroxide by microbial catalases by producing iodine-thiocyanate complexes prior to contact with microorganisms, with the aim of being able to decontaminate the ex vivo dentures colonized by yeasts.

Materials And Methods: Teabags containing lactoperoxidase adsorbed on inert clay beads were immersed for 1 minute in phosphate buffer solution (0.

Reaction Product Variability and Biological Activity of the Lactoperoxidase System Depending on Medium Ionic Strength and pH, and on Substrate Relative Concentration.

The potential of ions produced in water by the lactoperoxidase system against plant pests has shown promising results. We tested the bioactivity of ions produced by the lactoperoxidase oxidation of I and SCN in several buffers or in tap water and characterized the ions produced. In vitro biological activity was tested against Penicillium expansum, the causal agent of mold in fruits, and the major cause of patulin contamination of fruit juices and compotes.

Mode of action of lactoperoxidase as related to its antimicrobial activity: a review.

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.

Development of a colorimetric method for the dosage of OI- anions and I2 in aqueous media.

Lactoperoxidase catalyzes the oxidation of thiocyanate (SCN-) and iodide (I-) in presence of hydrogen peroxide in hypothiocyanite (OSCN-) ions and, depending on the pH, in hypoiodite (OI-) ions or in iode (I2). Oxidized SCN- and I- are part of the lactoperoxidase system, which is a natural biological protection in cow milk, and are described as having inhibitory properties against pathogenic human bacteria, fungi and viruses. We have developed an aqueous solution containing only OSCN- and OI- ions (without the enzyme) and we tested it successfully against plant pathogens.