title: Production and application of a rare disaccharide using sucrose phosphorylase from Leuconostoc mesenteroides.
abstract: Sucrose phosphorylase (SPase) from Leuconostoc mesenteroides exhibited activity towards eight ketohexoses, which behaved as D-glucosyl acceptors, and α-D-glucose-1-phosphate (G1P), which behaved as a donor. All eight of these ketohexoses were subsequently transformed into the corresponding d-glucosyl-ketohexoses. Of the eight ketohexoses evaluated in the current study, d-allulose behaved as the best substrate for SPase, and the resulting d-glucosyl-d-alluloside product was found to be a non-reducing sugar with a specific optical rotation of [α]D(20) + 74.36°. D-Glucosyl-D-alluloside was identified as α-D-glucopyranosyl-(1→2)-β-D-allulofuranoside by NMR analysis. D-Glucosyl-D-alluloside exhibited an inhibitory activity towards an invertase from yeast with a Km value of 50 mM, where it behaved as a competitive inhibitor with a Ki value of 9.2 mM. D-Glucosyl-D-alluloside was also successfully produced from sucrose using SPase and D-tagatose 3-epimerase. This process also allowed for the production of G1P from sucrose and d-allulose from D-fructose, which suggested that this method could be used to prepare d-glucosyl-d-alluloside without the need for expensive reagents such as G1P and d-allulose.
authors.affiliation: Rare Sugar Research Center, Kagawa University, Miki-cho, Kagawa 761-0795, Japan. Electronic address: morimoto@ag.kagawa-u.ac.jp.
authors.forename: Kenji
authors.initials: K
authors.lastname: Morimoto
authors.affiliation: Rare Sugar Research Center, Kagawa University, Miki-cho, Kagawa 761-0795, Japan.
authors.forename: Akihide
authors.initials: A
authors.lastname: Yoshihara
authors.affiliation: Faculty of Agriculture, Kagawa University, Miki-cho, Kagawa 761-0795, Japan.
authors.forename: Toshio
authors.initials: T
authors.lastname: Furumoto
authors.affiliation: Rare Sugar Research Center, Kagawa University, Miki-cho, Kagawa 761-0795, Japan.
authors.forename: Goro
authors.initials: G
authors.lastname: Takata
mesh_terms: D001667:Binding, Competitive; D002238:Carbohydrate Epimerases / Q000378:metabolism; D004187:Disaccharides / Q000096:biosynthesis* / Q000737:chemistry; D005632:Fructose / Q000378:metabolism; D005958:Glucosephosphates / Q000378:metabolism; D005964:Glucosyltransferases / Q000378:metabolism*; D006601:Hexoses / Q000737:chemistry / Q000378:metabolism*; D007934:Leuconostoc / Q000201:enzymology*; D009682:Magnetic Resonance Spectroscopy; D009904:Optical Rotation; D013379:Substrate Specificity; D013395:Sucrose / Q000378:metabolism; D043324:beta-Fructofuranosidase / Q000037:antagonists & inhibitors / Q000378:metabolism
chemical_list: D004187:Disaccharides; D005958:Glucosephosphates; D006601:Hexoses; C003243:psicose; D005632:Fructose; D013395:Sucrose; C031590:glucose-1-phosphate; D005964:Glucosyltransferases; C025901:sucrose phosphorylase; D043324:beta-Fructofuranosidase; D002238:Carbohydrate Epimerases; C030192:tagatose
keywords: Invertase inhibition; Rare disaccharide; Sucrose phosphorylase; d-Glucosyl-d-alluloside; d-Tagatose 3-epimerase