Interactions between hyaluronic acid, lysozyme, and the glucose oxidase-mediated lactoperoxidase system in enzymatic and candidacidal activities

ObjectiveTo investigate interactions between hyaluronic acid (HA), lysozyme, and the glucose oxidase-mediated lactoperoxidase (GO-LPO) system in enzymatic and candidacidal activities.DesignThe influences of HA (0.5, 1.0, and 2.0 mg/mL) and lysozyme (30 μg/mL hen egg white lysozyme) on the enzymatic activity of GO-LPO system (25 μg/mL bovine LPO, 1 mM KSCN, 10 units/mL GO, and 30 μg/mL glucose) were determined by measuring oxidized o-dianisidine production. The influence of the GO-LPO system on lysozyme activity was determined by measuring the turbidity of a Micrococcus lysodeikticus suspension. The effects of interactions between HA, lysozyme, the GO-LPO system on candidacidal activity were examined by pre-incubating various combinations of components. Candidacidal activity was determined by comparing the numbers of colony forming units using Candida albicans ATCC strains 10231, 18804, and 11006.ResultsHA inhibited the enzymatic activity of the GO-LPO system in a dose-dependent manner. HA inhibited the candidacidal activities of the GO-LPO system. However, the inhibitory activity of HA was not significantly different according to concentration of HA. The GO-LPO system enhanced the enzymatic activity of lysozyme, though lysozyme did not affect the enzymatic activity of the GO-LPO system. The candidacidal activities of the GO-LPO system and lysozyme were not additive.ConclusionsHA inhibited the enzymatic and candidacidal activity of the GO-LPO system. The GO-LPO system enhanced the enzymatic activity of lysozyme, but the candidacidal activities were not additive.