Open AccessBiosynthesis of glyceride glycoside (nonionic surfactant) by amylosucrase, a powerful glycosyltransferase
Author(s) -
YeJin Kim,
Ige i Siziya,
Seungpyo Hong,
Gil-Yong Lee,
Myung-Ji Seo,
Young-Rok Kim,
SangHo Yoo,
Cheon-Seok Park,
Dong-Ho Seo
Publication year - 2021
Publication title -
food science and biotechnology/food science and biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.595
H-Index - 38
eISSN - 2092-6456
pISSN - 1226-7708
DOI - 10.1007/s10068-020-00861-0
Subject(s) - chemistry , glycoside , glyceride , chromatography , stereochemistry , organic chemistry , biochemistry , fatty acid
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.