ENZYMATIC PRODUCTION OF BETA-THUJAPLICIN 2-O-BETA-D-GLUCOSIDE IN A MEMBRANE REACTOR USING AN INSOLUBLE UDP-GLUCOSYLTRANSFERASE FRACTION FROM CULTURED-CELLS OF EUCALYPTUS-PERRINIANA

Citation
N. Nakajima et al., ENZYMATIC PRODUCTION OF BETA-THUJAPLICIN 2-O-BETA-D-GLUCOSIDE IN A MEMBRANE REACTOR USING AN INSOLUBLE UDP-GLUCOSYLTRANSFERASE FRACTION FROM CULTURED-CELLS OF EUCALYPTUS-PERRINIANA, Journal of fermentation and bioengineering, 84(5), 1997, pp. 455-460
Citations number
26
ISSN journal
0922338X
Volume
84
Issue
5
Year of publication
1997
Pages
455 - 460
Database
ISI
SICI code
0922-338X(1997)84:5<455:EPOB2I>2.0.ZU;2-E
Abstract
Four UDP-glucosyltransfease (GTF) fractions were separated from the cu ltured cells of Eucalyptus perriniana, all of which exclusively produc ed beta-thujaplicin 2-O-beta-D-glucoside from beta-thujaplicin (hinoki tiol) in the presence of UDP-glucose (UDPG) as the sole glucose donor. An effective enzymatic system for repeated production of the monogluc oside has been developed by using an enzyme fraction as a water-insolu ble biocatalyst in an enzyme membrane reactor (slurry reactor) equippe d with an ultrafiltration membrane. The GTF also catalyzed the regiose lective glucosylation of salicyl alcohol to salicin and of various pol yphenols to naturally occurring pigments such as sugar-containing flav onoids. This study is the first to observe GTF activity in the enzyme fractions from the cultured cells of E. perriniana, which specifically catalyze the UDPG-dependent monoglucosylation of aromatic compounds a nd flavonoids.