Summary: Extracellular glucosyltransferases (sucrose: 1,6-α-D-glucan 3-α-and 6-α-glucosyltransferase) of HS6 (serotype ) were purified from the culture supernatant by DEAE-Sepharose chromatography, ConA-Sepharose chromatography and chromatofocusing. The enzymes I and II with specific activities of 6.20 and 5.86 i.u. mg, respectively, exhibited slightly different isoelectric points (pI 4.5 and 4.2) and the molecular weights were estimated to be 161000 and 174000, respectively, by SDS-PAGE. The enzymes had the same optimum pH of 5.5 and the same values of 1.3 mM for sucrose and of 83 μM-glucose equivalent for dextran T10. By double immunodiffusion test on agar, these enzymes were immunologically identical to each other. Analysis by GLC of the glucans synthesized from sucrose by the enzymes (I and II) established that they were 1,6-α-D-glucans with 20 and 24.5 mol% 1,3,6-branch points, respectively. Both are therefore Afunctional enzymes.


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