Affiliation:
1. Department of Microbiology, Hiroshima University School of Dentistry, Hiroshima 734, Japan
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
K
m
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.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
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