Abstract
Enzyme extracts or growing cells of Sporobolomyces singularis catalyzed glycosyl transfer from cellobiose or lactose to polyhydroxylic acceptors. The substituted hydroxyl, in each instance, had hydroxylic neighbors which appeared to have a role in the reaction. To show whether the pyranoid ring oxygen of glycosyl acceptors has an effect on the reaction, the substitution positions on pyranoid and myo-inositol acceptors are compared. Glucosyl transfer to the 1- and 5-positions of (1R)-myo-inositol3 and galactosyl transfer to the 5-position occurs. The configuration of hydroxyl groups adjacent to the position substituted is the same in these products as in the corresponding pyranoid derivatives. The pyranoid ring oxygen, therefore, has little effect on the glycosyl transfer reactions.
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