Acceptor Specificity of 4-α-Glucanotransferase from Pyrococcus kodakaraensis KOD1, and Synthesis of Cycloamylose

概要

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4-α-Glucanotransferase from a hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1 showed a broad acceptor specificity to various saccharides in an intermolecular transglycosylation reaction. In particular, the enzyme produced large amounts of transfer products of various acceptors such as D-glucose, methyl-α-_D-glucoside, phenyl-α-_D-glucoside, and _D-xylose. It is suggested that the requirement for an effective acceptor in the intermolecular transglycosylation reaction catalyzed by this enzyme is the pyranose stracture with the same configurations of the free C2-, C3-, and C4-hydroxyl groups as _D-glucopyranose, like cyclomaltodextringlucanotransferase (CGTase). However, the enzyme showed some acceptor specificities unlike those of CGTase. Analysis of the action of 4-α-glucanotransferase indicated that the enzyme catalyzes an intramolecular transglycosylation (cyclization) reaction of amylose to produce cyclic α-i, 4-glucan (cycloamylose). The yield of cycloamylose reached 67%, and the degree of polymerization was found to range from 16 to above 55.
社団法人日本生物工学会の論文
2000-10-25