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Purification and characterization of basic glucosyltransferase from Streptococcus mutans serotype c.

H Mukasa·A Shimamura·H Tsumori
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Abstract

Streptococcus mutans Ingbritt (serotype c) was found to secrete basic glucosyltransferase (sucrose: 1,6-alpha-D-glucan 3-alpha and 6-alpha-glucosyltransferase). The enzyme preparation obtained by ethanol fractionation, DEAE Bio-Gel A chromatography, chromatofocusing and preparative isoelectric focusing was composed of three isozymes with slightly different isoelectric points (pI 8.1-8.4). The molecular weight was estimated to be 151000 by SDS-polyacrylamide gel electrophoresis. The specific activity of the enzyme was 9.8 IU per mg of protein and the optimum pH was 6.5. The enzyme was activated 2.4-fold by commercial dextran T10, and had Km values of 7.1 micro M for the dextran and 4.3 mM for sucrose. Glucan was de novo synthesized from sucrose by the enzyme and found to be 1,6-alpha-D-glucan with 17.7% of 1,3,6-branching structure by a gas-liquid chromatography-mass spectroscopy.

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Chromatography, Ion ExchangeGlucosyltransferasesHydrogen-Ion ConcentrationIsoelectric FocusingKineticsStreptococcus mutansJournal Article

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H Mukasa, A Shimamura, H Tsumori. 1982-10-28. Purification and characterization of basic glucosyltransferase from Streptococcus mutans serotype c.. https://doi.org/10.1016/0304-4165(82)90310-5

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