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Updated: Oct 5, 2026

Purification of a High Molecular Mass Protein in Streptococcus mutans
Published on: September 14, 2019
Purification and characterization of an oligo-isomaltosaccharide synthase from a Streptococcus sobrinus
N Shinozaki-Kuwahara1, M Hayakawa, T Shiroza
1Department of Microbiology, Nihon University school of Dentistry at Matsudo, Chiba, Japan. nshino@mascat.nihon-u.ac.jp
Abstract:
One glucosyltransferase (GTF) -I deficient mutant of Streptococcus sobrinus strain B13N was isolated through chemical mutagenesis with ethyl methanesulfonate, and characterized. This mutant, designated as B13N-Id, readily allowed us to purify a homogeneous oligo-isomaltosaccharide synthase (GTF-S) from its culture fluid. The purified GTF-S was only recognized with rabbit polyclonal antibody against recombinant GTF-S from an Ecsherichia coli MD124 clone expressing the B13N gtfS gene, and showed the almost same enzymatic properties as the recombinant enzyme. A double reciprocal plot of the B13N GTF-S for sucrose was biphasic, and the affinity for this substrate was high compared to that of GTF-S enzymes from other strains.
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