earticle

논문검색

Poster-1

One-pot Enzymatic Synthesis of UDP-D-glucose based on immobilization

초록

영어

UDP-D-glucose is then used as a glucosyl donor for the biosynthesis of various carbohydrates, such as the cell envelope of Escherichia coli, lipopolysaccharide, capsular polysaccharide, and membranederived oligosaccharides. In addition, it is an essential intermediate for the growth on galactose and trehalose, including the synthesis of rehalose. UDP-D-glucose is also considered to be the glucosyl donor for glycogen synthesis in mammalian cells, but ADP-D-glucose or UDP-D-glucose can serve as glucosyl donors in eukaryotic microorganisms and plants. So to synthesize UDP-glucose from UMP via UDP and UTP, three enzymes TMK (thymidine monophosphate kinase), ACK (acetate kinase) and Gal-U (Glucose-1-phosphate uridylyltransferase gene) are needed. a one-pot reaction system with ATP regeneration was designed, in which easily available UMP and glucose-1-phosphate were used as starting materials. Enzyme immobilization is a method to keep enzyme molecules cofined or localized in a certain defined region of space with retention of their catalytic activities. In comparison with their native form, immobilized enzymes offer several advantages, such as enhanced stability, easier product recovery and purification, the possibility of repeated usage, and continuous process technology. so UDP-glucose synthase was immobilized as a cross-linked enzyme aggregate (CLEA) via precipitation with ammonium sulfate and cross-linking with glutaraldehyde. The effects of precipitation and cross-linking on CLEA activity were investigated and the immobilized enzymes were characterized.

저자정보

  • Mi-Ra Park Department of Pharmaceutical Engineering, Sunmoon University
  • Eui Min Kim Department of Pharmaceutical Engineering, Sunmoon University
  • Jae Kyung Song Department of Pharmaceutical Engineering, Sunmoon University

참고문헌

자료제공 : 네이버학술정보

    함께 이용한 논문

      ※ 원문제공기관과의 협약기간이 종료되어 열람이 제한될 수 있습니다.

      0개의 논문이 장바구니에 담겼습니다.