Intermolecular Transglycosylating Reaction of Cyclodextrin Glucanotransferase Immobilized on Capillary Membrane

概要

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The intermolecular transglucosylating reaction of cyclodextrin glucanotransferase ([EC 2.4.1.19]; CGTase) immobilized on a capillary membrane was investigated using low molecular weight substrayes such as cyclodextrin(CD), maltooligosaccharide (MOS), and a CD-MOS mixrture. The immobilized CGTase catalyzed the conversion reaction of α-CD to β-CD and MOS or β-CD to α-CD and MOS within a short residence time. The conversion ratio increased as the amount of immobilized CGTase increase. The addition of glucose, maltose, and sucrose as acceptors in the substrate solution containing CD resulted in the acceleration of CD degradation compared with ouly CD substrate. Furthermore, the MOS substraye (degree of polymerization=2-6) was disproportionated with a conversion ratio exceeding 70% by the immobilized CGTase. These data demonstrate that immobilized CGTase can catalyze intermolecular transglycosylation between low molecular substrates in a few minutes by resulating the amont of immobilized enzyme and the residence time. Thei might contribute to out comprehension of CGTase-immobilized bioreactors for CD productions as well as to the development of new glycosides through its excellent transglycosylation ability.
社団法人日本生物工学会の論文
1994-03-25