TRANSGLYCOSYLATION TO HESPERIDIN BY CYCLODEXTRIN GLUCANOTRANSFERASE FROM AN ALKALOPHILIC BACILLUS SPECIES IN ALKALINE PH AND PROPERTIES OF HESPERIDIN GLYCOSIDES
T. Kometani et al., TRANSGLYCOSYLATION TO HESPERIDIN BY CYCLODEXTRIN GLUCANOTRANSFERASE FROM AN ALKALOPHILIC BACILLUS SPECIES IN ALKALINE PH AND PROPERTIES OF HESPERIDIN GLYCOSIDES, Bioscience, biotechnology, and biochemistry, 58(11), 1994, pp. 1990-1994
Cyclodextrin glucanotransferase [1,4-alpha-D-glucan 4-alpha-D-(1,4-glu
cano)-transferase, cyclizine; CGTase, EC 2.4.1.19] from an alkalophili
c Bacillus species produced hesperidin monoglucoside and a series of i
ts oligoglucosides by the transglycosylation reaction with hesperidin
as an acceptor and soluble starch as a donor. The formation of the gly
cosides was more effective at alkaline pHs than at neutral or acidic p
Hs, because of higher solubility of the acceptor. The structure of the
purified monoglucoside was identified as 4(G)-alpha-D-glucopyranosyl
hesperidin by FAB-MS, alpha-, beta-glucosidase and glucoamylase treatm
ents, and methylation analysis. The solubility of both hesperidin mono
and diglucoside in water was about 300 times higher than that of hesp
eridin, and they were found to have a stabilizing effect on the yellow
pigment crocin, from fruits of Gardenia jasminoides, against ultravio
let radiation.