A System for Sialic Acid Transfer by Colominic Acid and a Sialidase that Preferentially Hydrolyzes Sialyl α-2,8 Linkages

概要

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A partially purified sialidase that preferentially hydrolyzes colominic acid, which is a homopolymer of N-Acetylneuraminic acid linked by α-2, 8 linkages, was prepared from Bacteroidesfragilis SBT3182. This enzyme had a K_m of 0. 63mM for α-2, 3-sialyllactose, 0. 97mM for α-2, 6-sialyllactose, and 0.01mM for colominic acid. Colominic acid was a good substrate of this enzyme. By using this kinetic property of the enzyme, we transferred sialic acid from colominic acid to lactose by the transferase activity of the sialidase. Both α-2, 3-sialyllactose and α-2, 6-sialyllactose were synthesized with a total yield of 0.14%. We also observed that the ratio of synthesized sialyllactose isomers changed with the reaction time while the yield was constant.
社団法人日本農芸化学会の論文
1995-04-23