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Catalytic properties of beta-cyclodextrin glucanotransferase from alkalophilic Bacillus sp BL-12 and intermolecular transglycosylation of stevioside


Catalytic properties of beta-cyclodextrin glucanotransferase from alkalophilic Bacillus sp BL-12 and intermolecular transglycosylation of stevioside



Biotechnology and Bioprocess Engineering 12(3): 207-212



ISSN/ISBN: 1226-8372

The catalytic properties of beta-cyclodextrin glucanotransferase (beta-CGTase) from alkalophilic Bacillus sp. BL-12 specific for the intermolecular transglycosylation of stevioside were investigated. The molecular mass of purified beta-CGTase by ultra-filtration and beta-cyclodextrin polymer affinity chromatography was estimated to be 90 kDa, which is high compared to other known bacterial CGTases. The optimal pH and temperature were 9.0 and 50 degrees C, respectively, and thermal stability at 40 degrees C was elevated 10-fold in the presence of 1% maltodextrin. The kinetic parameters of the new beta-CGTase from alkalophilic Bacillus sp. BL-12 indicate that it is more suitable for transglycosylation than the cyclization reaction. Maltodextrin was the most suitable glycosyl donor for transglycosylation of stevioside. The transglycosylation of stevioside was carried out using 60 units of CGTase per gram of maltodextrin, 20 g/L stevioside as the glycosyl acceptor, and 50 g/L maltodextrin as the glycosyl donor at 40 degrees C for 6 h, and a conversion yield of stevioside as high as 76% was obtained. (c) KSBB

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Accession: 015218996

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