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pH dependent effects of sodium ions on dextransucrase activity in Streptococcus mutans .

Authors :
Rather SA
Sharma SC
Mahmood A
Source :
Biochemistry and biophysics reports [Biochem Biophys Rep] 2019 Oct 07; Vol. 20, pp. 100692. Date of Electronic Publication: 2019 Oct 07 (Print Publication: 2019).
Publication Year :
2019

Abstract

Dextransuccrase (E.C 2.4.1.5) is a key enzyme in S. mutans for the metabolism of sucrose which helps in the adherence and accumulation of bacteria on tooth surface leading to the formation of dental caries. Dextransuccrase resembles in its catalytic properties with the brush boarder sucrase and exhibits pH dependent inhibitory and stimulatory effects in response to Na <superscript>+</superscript> . In this communication we studied the effect of monovalent cations on the activity of dextransuccrase from S. mutans . The percentage inhibition of dextransuccrase was 65% at 0.5 mM NaCl which enhanced to 90% at 20 mM sodium concentration. However there was no effect on dextransucrase activity in presence of other monovalent cations (Rb <superscript>+</superscript> , Cs <superscript>+</superscript> , and K <superscript>+</superscript> ) tested. Enzyme activity was enhanced 20-24% in acidic pH but was strongly inhibited (59-89%) around neutral and alkaline pH by 0.5-2.0 mM sodium chloride. Upon dialysis, 86% of enzyme activity was restored to control values. There was no effect of 2 mM NaCl on glucosyltransferase activity of the enzyme. Kinetic studies revealed that enzyme showed biphasic effects in response to Na <superscript>+</superscript> ions. At acidic pH the enzyme exhibited mixed type of activation affecting both Vmax and Km, while in alkaline pH, the enzyme showed V- type effect reducing Vmax by 74% without affecting Km. The effects of sodium ions on dextransuccrase activity were specific, thus it can be useful to block its catalytic activity, and reducing the cariogenic potential of S. mutans.<br />Competing Interests: All authors who contributed substantially to the work and participated in the writing of the manuscript, have seen and approved the revised version of this article and no part of the work has been published before. All authors declare that there is no conflict of interest with the contents of this article.<br /> (© 2019 Published by Elsevier B.V.)

Details

Language :
English
ISSN :
2405-5808
Volume :
20
Database :
MEDLINE
Journal :
Biochemistry and biophysics reports
Publication Type :
Academic Journal
Accession number :
31650041
Full Text :
https://doi.org/10.1016/j.bbrep.2019.100692