Food Science and Biotechnology

Korean Society of Food Science and Technology (한국식품과학회)
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Enzymatic Synthesis of Novel $\alpha$-Amylase Inhibitors via Transglycosylation by Thermotoga maritima Glucosidase

  • Kim, Sung-Hee (Center for Agricultural Biomaterials and Department of Food Science and Biotechnology, School of Agricultural Biotechnology, Seoul National University) ;
  • Lee, Myoung-Hee (Center for Agricultural Biomaterials and Department of Food Science and Biotechnology, School of Agricultural Biotechnology, Seoul National University) ;
  • Yang, Sung-Jae (Center for Agricultural Biomaterials and Department of Food Science and Biotechnology, School of Agricultural Biotechnology, Seoul National University) ;
  • Kim, Jung-Woo (Center for Agricultural Biomaterials and Department of Food Science and Biotechnology, School of Agricultural Biotechnology, Seoul National University) ;
  • Cha, Hyun-Ju (Center for Agricultural Biomaterials and Department of Food Science and Biotechnology, School of Agricultural Biotechnology, Seoul National University) ;
  • Cha, Jae-Ho (Department of Microbiology, Pusan National University) ;
  • Nguyen, Van Dao (Faculty of Biotechnology, Hanoi Open University) ;
  • Park, Kwan-Hwa (Center for Agricultural Biomaterials and Department of Food Science and Biotechnology, School of Agricultural Biotechnology, Seoul National University)
  • Published : 2008.04.30
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Abstract

Novel amylase inhibitors were synthesized via transglycosylation by Thermotoga maritima glucosidase (TMG). TMG hydrolyzes acarbose, acarviosine-glucose, and maltooligosaccharide by releasing $^{14}C$-labeled glucose from the reducing end of each molecule. When TMG was incubated with acarviosine-glucose (the donor) and glucose (the acceptor), two major transfer products, compounds 1 and 2, were formed via transglycosylation. The structures of the transfer products were determined using thin-layer chromatography (TLC), high-performance ion chromatography (HPIC), and $^{13}C$ nuclear magnetic resonance (NMR) spectroscopy. The results indicate that acarviosine was transferred to glucose at either C-6, to give a $\alpha-(1{\rightarrow}6$) glycosidic linkage, or at C-3, to produce an $\alpha-(1{\rightarrow}3$) glycosidic linkage. The transfer products showed a mixed-type inhibition against porcine pancreatic $\alpha$-amylase; therefore, they may be useful not only as inhibitors but also as acarbose transition-state analogs to study the mechanism of amylase inhibition.

Keywords

References

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