Efficient biotransformation of naringenin to naringenin α-glucoside, a novel α-glucosidase inhibitor, by amylosucrase from Deinococcus wulumuquiensis.

Autor: Yu SJ; Department of Food Science and Technology, College of Agriculture and Life Sciences, Jeonbuk National University, Jeonju 54896, Republic of Korea., So YS; Department of Food Science and Technology, College of Agriculture and Life Sciences, Jeonbuk National University, Jeonju 54896, Republic of Korea., Lim C; School of Pharmacy and Institute of New Drug Development, Jeonbuk National University, Jeonju 54896, Republic of Korea., Cho CH; Division of Functional Food Research Group, Korea Food Research Institute, Wanju 55365, Republic of Korea., Lee SG; Department of Food Science and Nutrition, Pukyong National University, Busan 48513, Republic of Korea., Yoo SH; Department of Food Science & Biotechnology and Carbohydrate Bioproduct Research Center, Sejong University, Seoul 05006, Republic of Korea., Park CS; Department of Food Science and Biotechnology, Graduate School of Biotechnology and Institute of Life Science and Resources, Kyung Hee University, Yongin 17104, Republic of Korea., Lee BH; Department of Food Science and Biotechnology, College of BioNano Technology, Gachon University, Seongnam 13120, Republic of Korea., Min KH; School of Pharmacy and Institute of New Drug Development, Jeonbuk National University, Jeonju 54896, Republic of Korea. Electronic address: khmin1492@jbnu.ac.kr., Seo DH; Department of Food Science and Technology, College of Agriculture and Life Sciences, Jeonbuk National University, Jeonju 54896, Republic of Korea; Department of Food Science & Biotechnology and Carbohydrate Bioproduct Research Center, Sejong University, Seoul 05006, Republic of Korea; Department of Food Science and Biotechnology, Graduate School of Biotechnology and Institute of Life Science and Resources, Kyung Hee University, Yongin 17104, Republic of Korea. Electronic address: dhseo@khu.ac.kr.
Jazyk: angličtina
Zdroj: Food chemistry [Food Chem] 2024 Aug 01; Vol. 448, pp. 139182. Date of Electronic Publication: 2024 Mar 30.
DOI: 10.1016/j.foodchem.2024.139182
Abstrakt: Amylosucrase (ASase) efficiently biosynthesizes α-glucoside using flavonoids as acceptor molecules and sucrose as a donor molecule. Here, ASase from Deinococcus wulumuqiensis (DwAS) biosynthesized more naringenin α-glucoside (NαG) with sucrose and naringenin as donor and acceptor molecules, respectively, than other ASases from Deinococcus sp. The biotransformation rate of DwAS to NαG was 21.3% compared to 7.1-16.2% for other ASases. Docking simulations showed that the active site of DwAS was more accessible to naringenin than those of others. The 217th valine in DwAS corresponded to the 221 st isoleucine in Deinococcus geothermalis AS (DgAS), and the isoleucine possibly prevented naringenin from accessing the active site. The DwAS-V217I mutant had a significantly lower biosynthetic rate of NαG than DwAS. The k cat /K m value of DwAS with naringenin as the donor was significantly higher than that of DgAS and DwAS-V217I. In addition, NαG inhibited human intestinal α-glucosidase more efficiently than naringenin.
Competing Interests: Declaration of competing interest All of the authors declare no conflicts of interest.
(Copyright © 2024 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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