Nigerose and nigerooligosaccharides served as accepters for a glucosyltrans
ferase GTF-I from cariogenic Streptococcus sobrinus to give a series of hom
ologous acceptor products. The soluble oligosaccharides (dp 5-9) strongly a
ctivated the acceptor reaction, resulting in the accumulation of water-inso
luble (1 --> 3)-alpha-D-glucan. The enzyme transferred the labeled glucosyl
residue from D-[U-C-13]sucrose to the 3-hydroxyl group at the non-reducing
end of the (1 --> 3)-alpha-D-oligosaccharides, as unequivocally shown by N
MR C-13-C-13 coupling patterns. The values of the C-13-C-13 one-bond coupli
ng constant ((1)J) are also presented for the C-1-C-6 of the C-13-labeled a
lpha-(1 --> 3)-linked glucosyl residue and of the non-reducing-end residue.
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