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
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
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.