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Food Science and Biotechnology
→ Food Science and Biotechnology 2021 ; 30(2): 267-276
Biosynthesis of glyceride glycoside (nonionic surfactant) by amylosucrase, a powerful glycosyltransferase
Ye-Jin Kim1 • Inonge Noni Siziya2 • Seungpyo Hong3 • Gil-Yong Lee4 • Myung-Ji Seo5 • Young-Rok Kim1 • Sang-Ho Yoo6 • Cheon-Seok Park1 • Dong-Ho Seo2,7,8
1 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 2 Department of Food Science and Technology, College of Agriculture and Life Sciences, Jeonbuk National University, Jeonju 54896, Republic of Korea 3 Research Group of Healthcare, Korea Food Research Institute, Wanju 55365, Republic of Korea 4 Healthcare Research Institute, Kolon Industries, Inc, Seoul 07793, Republic of Korea 5 Division of Bioengineering, Incheon National University, Incheon 22012, Republic of Korea 6 Department of Food Science and Biotechnology, and Carbohydrate Bioproduct Research Center, Sejong University, Seoul 05006, Republic of Korea 7 Department of Agricultural Convergence Technology, Jeonbuk National University, Jeonju 54896, Republic of Korea 8 Institute of Agricultural Science and Technology, Jeonbuk National University, Jeonju 54896, Republic of Korea
ABSTRACT
Amylosucrase (ASase, E.C. 2.4.1.4) is a powerful transglycosylation enzyme that can transfer glucose from sucrose to the hydroxyl (-OH) group of various compounds. In this study, recombinant ASases from Deinococcus geothermalis (DgAS) and Bifidobacterium thermophilum (BtAS) were used to synthesize biosurfactants based on the computational analysis of predicted docking simulations. Successful predictions of the binding affinities, conformations, and three-dimensional structures of three surfactants were computed from receptor-ligand binding modes. DgAS and BtAS were effective in the synthesis of biosurfactants from glyceryl caprylate, glyceryl caprate, and polyglyceryl-2 caprate. The results of the transglycosylation reaction were consistent for both ASases, with glyceryl caprylate acceptor showing the highest concentration, as confirmed by thin layer chromatography. Furthermore, the transglycosylation reactions of DgAS were more effective than those of BtAS. Among the three substrates, glyceryl caprylate glycoside and glyceryl caprate glycoside were successfully purified by liquid chromatography– mass spectrometry (LC–MS) with the corresponding molecular weights.
KEYWORD
Amylosucrase · Biosurfactant · Docking simulation · Glyceryl glycoside · Transglycosylation
Food Science and Biotechnology 2021 ; 30(2): 267-276
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