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. 1974 Jun;118(3):796–804. doi: 10.1128/jb.118.3.796-804.1974

Purification and Properties of Dextransucrase and Invertase from Streptococcus mutans

Kazuhiro Fukui 1, Yoshio Fukui 1, Takafumi Moriyama 1
PMCID: PMC246824  PMID: 4133613

Abstract

Invertase (β-d-fructofuranoside fructohydrolase, EC 3.2.1.26) and dextransucrase (α-1, 6-glucan: d-fructose 2-glucosyltransferase, EC 2.4.1.5) were purified from the culture fluids of Streptococcus mutans by chromatography on Sepharose 6B and diethylaminoethyl-cellulose followed by treatment with hydroxyapatite. Each of the enzyme preparations gave a single band when analyzed by either polyacrylamide gel electrophoresis or immunodiffusion. The antigenic determinant of invertase was different from that of dextransucrase on immunodiffusion. The pH optima were 5.25 for invertase and 5.75 for dextransucrase, and the Km values were 20 mM for invertase and 2.0 mM for dextransucrase. The molecular weights determined by sodium dodecyl sulfate gel electrophoresis were 160,000 for invertase and 170,000 for dextransucrase. The data obtained suggest that the dextransucrase had dextran-synthesizing activity and invertase-like activity.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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