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Title: Purification and characterization of an oligo-isomaltosaccharide synthase from a Streptococcus sobrinus glucosyltransferase-I deficient mutant. Author: Shinozaki-Kuwahara N, Hayakawa M, Shiroza T, Abiko Y, Fukushima K. Journal: Biosci Biotechnol Biochem; 2001 Jun; 65(6):1290-5. PubMed ID: 11471726. 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.[Abstract] [Full Text] [Related] [New Search]