The effect of increased mastication on plaque metabolism and salivary gland function was determined in 11 human subjects who chewed a sugarless gum for ten minutes of each waking hour for two weeks. Prior to and at the conclusion of the gum-chewing regimen, unstimulated whole saliva and 2% citric-acid-stimulated parotid saliva were collected. Flow rates, pH, and buffer capacity were determined on all saliva samples. In addition, parotid saliva was analyzed for protein concentration and the proteins further studied by SDS-PAGE. The plaque pH response to a 10% sucrose rinse was also measured before and after the regimen. Significant increases were observed in the pH and buffer capacity of unstimulated whole saliva as were similar increases in the flow rate, pH, and buffer capacity of stimulated parotid saliva. Protein concentrations and profiles remained unaffected. In addition, the resting plaque pH and minimum plaque pH reached after a sucrose challenge were both raised significantly, with a significant reduction in the cH area. The results of this study indicate that increased masticatory effort by frequent consumption of sugar-free chewing gum over a prolonged time period resulted in a functional increase in the output of stimulated parotid saliva, as well as in increases in pH and buffer capacity of whole and parotid saliva, which may help to reduce plaque acidogenicity.
The plasmid pHG contains a cyclodextrin glycosyltransferase (CGTase) gene (cgt) derived from Bacillus macerans. Two transformants, Bacillus subtilis (pHG) and Escherichia coli (pHG), were found to produce CGTases with the same primary structure as the enzyme from B. macerans. However, the beta-cyclodextrin coupling activity of the CGTase from E. coli (pHG) was 14-fold higher than that of the enzymes from the other strains. By contrast, no differences in alpha-cyclodextrin coupling activities were observed among these CGTases. CGTase from E. coli (pHG) was found to be less thermostable than the other CGTases. When the CGTase produced by B. subtilis was treated with increasing urea concentrations (10-1000 mM) to promote increasing degrees of protein unfolding, a bell-shaped beta-cyclodextrin coupling activity profile was obtained. Subtle differences in the conformation of the CGTase produced by E. coli are therefore proposed to be responsible for the markedly increased beta-cyclodextrin coupling activity of this enzyme.
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