Summary: An extracellular glucosyltransferase (GT-S) synthesizing water-soluble glucan was purified from the culture supernatant of BHT (serotype , subsp. ) by DEAE-Sepharose chromatography and preparative isoelectric focusing. The 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), an optimum pH of 6·0 and a value of 0·8 m 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 and . The glucan synthesized 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.


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