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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)
Publication Information
Food Science and Biotechnology / v.17, no.2, 2008 , pp. 302-307 More about this Journal
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
Thermotoga maritima glucosidase (TMG); acarbose; transfer product; inhibition$\alpha$-amylase;
Citations & Related Records
Times Cited By KSCI : 2  (Citation Analysis)
Times Cited By Web Of Science : 2  (Related Records In Web of Science)
Times Cited By SCOPUS : 2
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