title: Interactions of streptococcal glucosyltransferases with alpha-amylase and starch on the surface of saliva-coated hydroxyapatite.
abstract: The salivary pellicle consists of various proteins and glycoproteins which may interact with one another. Experiments were performed to elucidate the interactions of streptococcal glucosyltransferase (Gtf) enzymes with human salivary alpha-amylase in solution and on the surface of saliva-coated hydroxyapatite (SHA) beads. The Gtf enzymes -B, -C and -D, when immobilized on to SHA beads, reduced the activity of adsorbed amylase; GtfD showed the highest inhibition of salivary amylase activity. The presence of glucan produced by immobilized GtfD did not further reduce amylase activity. The amount of amylase adsorbed on to hydroxyapatite beads was reduced when salivary amylase was added simultaneously with any of the Gtf enzymes, suggesting that amylase and Gtfs may compete with each other for binding sites on hydroxyapatite. Starch hydrolysates produced by SHA-surface-bound salivary amylase were tested for their effect on glucan production from sucrose by Gtf enzymes in solution and on SHA beads; glucan production by SHA-immobilized GtfB was stimulated in the presence of starch hydrolysates. Glucan synthesized by SHA-immobilized GtfB in the presence of starch hydrolysates was less susceptible to hydrolysis by the fungal enzyme mutanase than was glucan made by SHA-immobilized GtfB in the absence of starch hydrolysates. Glucan production by GtfB associated with streptococci immobilized on to SHA was also enhanced in the presence of starch hydrolysates. The adhesion of oral micro-organisms to SHA coated with glucan made in the presence and absence of starch hydrolysates was investigated, and some bacteria displayed higher adhesion activities for the glucan made in the presence of the hydrolysates. Therefore, the interaction of amylase and Gtf enzymes on a SHA surface may modulate the formation of glucan and the adherence of oral micro-organisms.
authors: Department of Dental Research, Rochester Caries Research Center, University of Rochester, NY 14642, USA.
authors: A M
authors: AM
authors: Vacca-Smith
authors: A R
authors: AR
authors: Venkitaraman
authors: R G
authors: RG
authors: Quivey
authors: W H
authors: WH
authors: Bowen
mesh_terms: D000327:Adsorption; D000328:Adult; D000681:Amylases / Q000378:metabolism*; D001422:Bacterial Adhesion / Q000502:physiology*; D001426:Bacterial Proteins / Q000378:metabolism; D001667:Binding, Competitive; D044622:Dental Pellicle; D003773:Dental Plaque / Q000378:metabolism*; D003910:Dextranase / Q000378:metabolism; D017886:Durapatite / Q000378:metabolism; D005260:Female; D005656:Fungal Proteins / Q000378:metabolism; D005936:Glucans / Q000096:biosynthesis; D005964:Glucosyltransferases / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000378:metabolism; D006801:Humans; D006868:Hydrolysis; D012463:Saliva / Q000201:enzymology; D012471:Salivary Proteins and Peptides / Q000378:metabolism*; D013213:Starch / Q000378:metabolism; D013291:Streptococcus / Q000201:enzymology*
chemical_list: D001426:Bacterial Proteins; D005656:Fungal Proteins; D005936:Glucans; D012471:Salivary Proteins and Peptides; D013213:Starch; D017886:Durapatite; D005964:Glucosyltransferases; D000681:Amylases; D006026:Glycoside Hydrolases; D003910:Dextranase; C021780:exo-1,3-alpha-glucanase