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 in | Journal of microbiology and biotechnology Vol. 17; no. 9; pp. 1550 - 1553 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Seoul
Korean Society for Applied Microbiology
01.09.2007
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Subjects | |
Online Access | Get full text |
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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%. |
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Bibliography: | A50 2008000468 ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 1017-7825 |