Functional characteristics of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. BL-31 highly specific for intermolecular transglycosylation of bioflavonoids.
The functional characteristics of a beta-cyclodextrin glucanotransferase (CGTase) excreted from alkalophilic Bacillus sp. BL-31 that is highly specific for the intermolecular transglycosylation of bioflavonoids were investigated. The new beta-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 degrees C for 6 h, resulting in a high conversion yield of 92.1%.
Department of Genetic Engineering, College of Natural Sciences, Kyungpook National University, Daegu 702-701, Korea.
Young-Hoon
YH
Go
Tae-Kwon
TK
Kim
Kwang-Woo
KW
Lee
Yong-Hyun
YH
Lee
D001407:Bacillus / Q000201:enzymology*; D002851:Chromatography, High Pressure Liquid; D044950:Flavanones / Q000378:metabolism; D005419:Flavonoids / Q000096:biosynthesis* / Q000378:metabolism; D005964:Glucosyltransferases / Q000302:isolation & purification* / Q000378:metabolism*; D006031:Glycosylation; D006569:Hesperidin / Q000378:metabolism; D015394:Molecular Structure; D012431:Rutin / Q000378:metabolism
D044950:Flavanones; D005419:Flavonoids; D012431:Rutin; D006569:Hesperidin; D005964:Glucosyltransferases; C019963:cyclomaltodextrin glucanotransferase; C005274:naringin