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Biosynthesis of glyceride glycoside (nonionic surfactant) by amylosucrase, a powerful glycosyltransferase.


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.

SUBMITTER: Kim YJ 

PROVIDER: S-EPMC7914313 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature

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Biosynthesis of glyceride glycoside (nonionic surfactant) by amylosucrase, a powerful glycosyltransferase.

Kim Ye-Jin YJ   Siziya Inonge Noni IN   Hong Seungpyo S   Lee Gil-Yong GY   Seo Myung-Ji MJ   Kim Young-Rok YR   Yoo Sang-Ho SH   Park Cheon-Seok CS   Seo Dong-Ho DH  

Food science and biotechnology 20210206 2


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 <i>Deinococcus geothermalis</i> (DgAS) and <i>Bifidobacterium thermophilum</i> (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 t  ...[more]

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