Surface versus bulk activity of lysozyme deposited on hydrogel contact lens materials in vitro

TitleSurface versus bulk activity of lysozyme deposited on hydrogel contact lens materials in vitro
Publication TypeJournal Article
Year of Publication2018
AuthorsOmali, N., L. Subbaraman, M. Heynen, A. Ng, C. Coles-Brennan, Z. Fadli, and L. Jones
JournalContact Lens and Anterior Eye
KeywordsArticle, artificial tear, bulk enzyme activity, comparative study, contact lens, controlled study, Denaturation, enzyme activity, etafilcon a, hydrogel, in vitro study, incubation time, lysozyme, nelfilcon a, nesofilcon A, nonhuman, ocufilcon, omafilcon a, polymacon, povidone, priority journal, Protein activity, surface enzyme activity, turbidity, unclassified drug

Purpose: To determine and compare the levels of surface versus bulk active lysozyme deposited on several commercially available hydrogel contact lens materials. Methods: Hydrogel contact lens materials [polymacon, omafilcon A, nelfilcon A, nesofilcon A, ocufilcon and etafilcon A with polyvinylpyrrolidone (PVP)] were incubated in an artificial tear solution for 16 h. Total activity was determined using a standard turbidity assay. The surface activity of the deposited lysozyme was determined using a modified turbidity assay. The amount of active lysozyme present within the bulk of the lens material was calculated by determining the difference between the total and surface active lysozyme. Results: The etafilcon A materials showed the highest amount of total lysozyme activity (519 ± 8 μg/lens, average of Moist and Define), followed by the ocufilcon material (200 ± 5 μg/lens) and these two were significantly different from each other (p < 0.05). The amount of surface active lysozyme on etafilcon and ocufilcon lens materials was significantly higher than that found on all other lenses (p < 0.05). There was no active lysozyme quantified in the bulk of the nelfilcon material, as all of the active lysozyme was found on the surface (1.7 ± 0.3 μg/lens). In contrast, no active lysozyme was quantified on the surface of polymacon, with all of the active lysozyme found in the bulk of the lens material (0.6 ± 0.6 μg/lens). Conclusions: The surface and bulk activity of lysozyme deposited on contact lenses is material dependent. Lysozyme deposited on ionic, high water content lens materials such as etafilcon A show significantly higher surface and bulk activity than many other hydrogel lens materials. © 2018 British Contact Lens Association