The diffusion and enzymic hydrolysis of monofluorophosphate in dental plaque.

Abstract

Although the ability of dental plaque to hydrolyze sodium monofluorophosphate (MFP) has been known for some time, its effect on the F- concentration at the plaque-enamel interface is undefined. We have determined enzyme kinetic values for MFP hydrolysis and diffusion coefficients so that the penetration and degradation of MFP in plaque can be modeled by computer. The KM and Vmax values for natural human plaque were 1.77 mmol/L and 41.4 nmol/min/mg protein, respectively, at pH 8.0. At pH 6.0, the Vmax was lower, 15.6 nmol/min/mg, but KM was not significantly different. Competitive inhibition by orthophosphate gave a Ki of 4.55 mmol/L. The diffusion coefficient for MFP in artificial plaque was 1.91 x 10(-6) cm2/sec. When these data were used for mathematical modeling of the effects of rinsing with MFP and F- solutions, compared with an equivalent NaF application, the concentration of F- from MFP was lower at the inner surface of plaque, and the peak occurred later. Both pH and plaque thickness had a marked effect on the amount of MFP that could penetrate: At pH 8.0, almost none reached the inner surface of a 1-mm-thick plaque intact. At pH 6.0, however, more MFP was able to penetrate, due to lower MFPase activity. While MFP diffusion is inherently slower than that of F-, enzymic degradation increases the gradient for inward diffusion. If the conventional view that MFP in toothpaste acts as a source of F- is true, then MFP toothpaste should be formulated to optimize MFPase activity in dental plaque.