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  • Title: Purification and characterization of extracellular glucosyltransferase from Streptococcus mutans serotype b (subspecies rattus).
    Author: Kumada H, Umemoto T, Onisi M, Tsumori H, Shimamura A, Mukasa H.
    Journal: J Gen Microbiol; 1987 Jun; 133(6):1435-41. PubMed ID: 2959747.
    Abstract:
    An extracellular glucosyltransferase (GT-S) synthesizing water-soluble glucan was purified from the culture supernatant of Streptococcus mutans BHT (serotype b, subsp. rattus) by DEAE-Sepharose chromatography and preparative isoelectric focusing. The Mr of the enzyme was 155,000 and the pI was 4.5. The GT-S had a specific activity of 10.2 i.u. (mg protein)-1, an optimum pH of 6.0 and a Km value of 0.8 mM for sucrose, and was activated twofold by dextran T10. The GT-S was immunologically partially identical with the corresponding enzymes in crude preparations from serotypes c, e and f. The glucan synthesized de novo from sucrose by the GT-S was water-soluble and consisted of 29 mol% of non-reducing terminal, 49 mol% of 1,6-alpha-linked, 11 mol% of 1,3-alpha-linked and 11 mol% of 1,3,6-alpha-branched glucose residues.
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