RT Journal Article SR Electronic(1) A1 FURUTA, TAKUSHI A1 KOGA, TOSHIHIKO A1 NISIZAWA, TOSIKI A1 OKAHASHI, NOBUO A1 HAMADA*, SHIGEYUKIYR 1985 T1 Purification and Characterization of Glucosyltransferases from Streptococcus mutans 6715 JF Microbiology, VO 131 IS 2 SP 285 OP 293 DO https://doi.org/10.1099/00221287-131-2-285 PB Microbiology Society, SN 1465-2080, AB Summary: A water-soluble glucan-synthesizing glucosyltransferase (GTase-S) and a water-insoluble glucan-synthesizing glucosyltransferase (GTase-I) were purified from culture supernatant of Streptococcus mutans 6715 (serotype g) by ammonium sulphate precipitation, chromatofocusing on a Polybuffer exchanger PBE 94 column, and subsequent phenyl-Sepharose CL-4B or hydroxyapatite column chromatography. The GTase-S and GTase-I activities were purified 4019- and 4714-fold, respectively, and the molecular weights were calculated to be 160000 and 165000, respectively. GTase-S had a pH optimum of 5·0, a K m of 8·8 mm for sucrose in the presence of 20μm-dextran T10, and an isoelectric point of pH 4·3. GTase-I had two pH optima of 5·0 and 7·0, K m values of 9·4 mm (at pH 5·0) and 7·0 mm (at pH 7·0), and an isoelectric point of pH 4·9. Methylation analysis indicated that the water-soluble glucan produced by GTase-S was a highly branched 1,6-α-linked d-glucan with 1,3-linked glucose residues, and that the water-insoluble glucan synthesized by GTase-I was composed of 1,3-α-linked glucose units., UL https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-131-2-285