Abstract
Cyclodextrin glucanotransferase (1, 4-α-d-glucan 4-α-d-(l, 4-α-d-glucano)-transferase (cyclizing), EC 2.4.1.19, CGTase) from an alkalophilic Bacillus species was purified by starch adsorption and Q-Sepharose chromatography. The purified enzyme had cyclizing activity, transglycosylating (coupling) activity, and starch-hydrolyzing activity, and their pH-activity curves had a single peak (pH 5.5 as the optimum pH) with a broad shoulder at alkaline pHs.Transglycosylation to various saccharides and flavonoids at alkaline pH was more effective than that at neutral pH. Among flavonoids, those containing rutinose (diosmin and hesperidin) were transglycosylated more effectively than those containing neohesperidose (naringin and neohesperidin).
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