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.
저자
Rit Bahadur Gurung [ Department of Pharmaceutical Engineering, Institute of Biomolecule Reconstruction, Sun Moon University ]
Jae Kyung Sohng [ Department of Pharmaceutical Engineering, Institute of Biomolecule Reconstruction, Sun Moon University ]
본 학회는 화학, 생화학, 분자생물학, 미생물학, 식품공학, 의학, 약학, 유전공학 및 생물공학, 환경 및 기타 공업 등 전 분야의 탄수화물관련 이론과 기술을 연구 발전시키고 산학협동을 통해 이를 보급하여 국내 관련 산업의 발전 및 국민생활의 과학화에 기여하고자 하며, 이러한 목표와 비젼의 실현을 위해 회원들이 적극적인 참여와 활동을 전개하고자 한다.