Effect of salts on water-insoluble glucan formation by glucosyltransferase of Streptococcus mutans.

Abstract:

:The formation of water-insoluble glucan by extracellular glucosyltransferase from Streptococcus mutans 6715 found to be greatly stimulated by various mono- or divalent cations. An enzyme preparation, obtained by ethanol fractionation, was able to catalyze the formation of water-insoluble glucan from sucrose in the presence of monovalent cations above 100mM or divalent cations above 20 mM at neutral pH. As the concentration of monovalent and divalent cations was reduced to below 10 mM and 1 mM, respectively, the formation of insoluble glucan decreased to a negligible amount. High concentrations of these cations were found to stimulate the formation of insoluble glucan in the following ways: (i) it increased the activity of total glucosyltransferase up to 1.6- and 2.7-fold in the absence and presence of a primer dextran, respectively, and (ii) it changed the formation of soluble glucan to insoluble. It was postulated that one of the essential factors for the formation of insoluble glucan would be to keep more than two water-soluble glucan chains close to enzyme aggregates and that such interaction could be enhanced by the presence of high cation concentrations.

journal_name

Infect Immun

journal_title

Infection and immunity

authors

Mukasa H,Shimamura A,Tsumori H

doi

10.1128/IAI.23.3.564-570.1979

subject

Has Abstract

pub_date

1979-03-01 00:00:00

pages

564-70

issue

3

eissn

0019-9567

issn

1098-5522

journal_volume

23

pub_type

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