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Enzyme extracts or growing cells of Sporobolomycessingulariscatalyzed 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-inositol3and 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.

The yeast, Rhodotorulaglutinis, gives an exocellular mannan containing 1,3-β- and 1.4-β-D-mannopyranose residues arranged in a straight chain of at least 90 units. Consecutive 1,3-β links are absent and although consecutive 1,4-β links may exist they are present at most in only a very small proportion. The 1,3-β- and 1,4-β-D-mannopyranose residues are therefore arranged alternately in the chain.Mannans from R. mucilaginosa, R. minuta, and an unidentified Rhodotorulaspp. 62-506 appear to have similar structures.