Functional Characteristics of Cyclodextrin Glucanotransferase from Alkalophilic Bacillus sp. BL-31 Highly Specific for Intermolecular Transglycosylation of Bioflavonoids

The functional characteristics of a β-cyclodextrin glucanotransferase (CGTase) excreted from alkalophilic Bacillus sp. BL-31 that is highly specific for the intermolecular transglycosylation of bioflavonoids were investigated. The new β-CGTase showed high specificities for glycosyl acceptor bioflavo...

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Published inJournal of microbiology and biotechnology Vol. 17; no. 9; pp. 1550 - 1553
Main Authors Go, Y.H. (Kyungpook National University, Daegu, Republic of Korea), Kim, T.K. (Kyungpook National University, Daegu, Republic of Korea), Lee, K.W. (Kyungpook National University, Daegu, Republic of Korea), Lee, Y.H. (Kyungpook National University, Daegu, Republic of Korea), E-mail: leeyh@knu.ac.kr
Format Journal Article
LanguageEnglish
Published Seoul Korean Society for Applied Microbiology 01.09.2007
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Summary:The functional characteristics of a β-cyclodextrin glucanotransferase (CGTase) excreted from alkalophilic Bacillus sp. BL-31 that is highly specific for the intermolecular transglycosylation of bioflavonoids were investigated. The new β-CGTase showed high specificities for glycosyl acceptor bioflavonoids, including naringin, rutin, and hesperidin, and especially naringin. The transglycosylation of naringin into glycosyl naringin was then carried out under the conditions of 80 units of CGTase per gram of maltodextrin, 5 g/l of naringin, 25 g/l of maltodextrin, and 1 mM Mn²+ ion at 40℃ for 6 h, resulting in a high conversion yield of 92.1%.
Bibliography:A50
2008000468
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ISSN:1017-7825