earticle

논문검색

Poster 05

Enzymatic glycosylation of select flavones using UDP-glucosyltransferase YjiC from BacilluslicheniformisDSM13

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.

저자정보

  • 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

참고문헌

자료제공 : 네이버학술정보

    함께 이용한 논문

      ※ 원문제공기관과의 협약기간이 종료되어 열람이 제한될 수 있습니다.

      0개의 논문이 장바구니에 담겼습니다.