원문정보
초록
영어
Glycosylation can significantly improve the water solubility, stability and thus increase bioavailability and enhance biological activity of low molecular weight organic compounds. Enzymatic glycosylation methods have several advantages over the classical methods of organic syntheses in terms of cost, efficiency and selectivity. The UDP-glucosyltransferase YjiC from Bacillus licheniformis DSM 13, a member of family 1 glycosyltransferase was expressed in Escherichia coli BL21 (DE3) as N-terminal hexahistidine-tagged fusion protein. Purified YjiC was used to glycosylate apigenin, baicalein, chrysin, diosmetin and luteolin. The products have been analyzed by high performance liquid chromatography (HPLC) and high resolution liquid chromatography-electrospray ionization-quadrupole-time of flight-mass spectrometry (HRLC-ESI-Q-TOF-MS) methods. The formation of mono and diglucosides has been reported with all the substrates. Even though glycosylation is preferred at positions other than C5 carbon of flavonoids whenever there is the presence of more than one phenolic hydroxyl groups, the promiscuity of YjiC was not observed. The exact position of glycosylation by YjiC is yet to be determined.