A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä

Lactoperoxidase inhibits glucosyltransferases from Streptococcus mutans in vitro




TekijätKorpela A, Yu X, Loimaranta V, Lenander-Lumikari M, Vacca-Smith A, Wunder D, Bowen WH, Tenovuo J

Julkaisuvuosi2002

JournalCaries Research

Tietokannassa oleva lehden nimiCaries research

Lehden akronyymiCaries Res

Vuosikerta36

Numero2

Aloitussivu116

Lopetussivu21

Sivujen määrä6

ISSN0008-6568

DOIhttps://doi.org/10.1159/000057869


Tiivistelmä
This study examines the possible effect of the antimicrobial peroxidase system on the activity of streptococcal glucosyltransferases B, C and D (GtfB, GtfC and GtfD), either in solution (GtfB and GtfC) or when adsorbed to hydroxyapatite (GtfC and GtfD) at pH 6.5. The lactoperoxidase (LP) system (LP, H(2)O(2), SCN(-)) had no effect on the activity of dissolved GtfC, but the activity of dissolved GtfB was enhanced. The LP system, however, strongly inhibited the activities of both GtfC and GtfD in their adsorbed form. LP enzyme, without its substrates, inhibited all three Gtf enzymes: GtfB and GtfC in concentrations between 10 and 100 microg/ml in liquid phase and adsorbed GtfC and GtfD in concentrations between 25 and 50 microg/ml. This inhibition was in part abolished in liquid phase, but not in solid phase, if the substrates of LP were added. This study shows that the lactoperoxidase system can exert inhibitory activity against streptococcal Gtfs without generating oxidizing agents.



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