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 M(r) of the enzyme was 155000 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 K(m) 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-α-linked, 11 mol% of 1,3-α-linked and 11 mol% of 1,3,6-α-branched glucose residues.
CITATION STYLE
Kumada, H., Umemoto, T., Onisi, M., Tsumori, H., Shimamura, A., & Mukasa, H. (1987). Purification and characterization of extracellular glucosyltransferase from Streptococcus mutans serotype b (subspecies rattus). Journal of General Microbiology, 133(6), 1435–1441. https://doi.org/10.1099/00221287-133-6-1435
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