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  • Title: Purification and properties of extracellular glucosyltransferase synthesizing 1,3-alpha-D-glucan from Streptococcus mutans serotype a.
    Author: Tsumori H, Shimamura A, Mukasa H.
    Journal: J Gen Microbiol; 1985 Mar; 131(3):553-9. PubMed ID: 3160820.
    Abstract:
    Extracellular 1,3-alpha-D-glucan synthase (sucrose: 1,3-alpha-D-glucan 3-alpha-D-glucosyltransferase, EC 2.4.1.-) of Streptococcus mutans HS6 (serotype a) was purified from culture supernatant by ultrafiltration, DEAE-Sepharose chromatography and preparative isoelectric focusing. The enzyme had a molecular weight of 158 000 by SDS-PAGE and an isoelectric point of pH 5.2. The specific activity of the enzyme was 48.3 i.u. (mg protein)-1. The Km for sucrose was 1.2 mM and the activity was optimal at pH 6.0. The enzyme activity was stimulated about 20-fold in the presence of dextran T10. Glucan was synthesized de novo from sucrose by the enzyme and characterized as a linear 1,3-alpha-D-glucan by GC-MS.
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