title: Enzymatic alpha-glucosaminylation of maltooligosaccharides catalyzed by phosphorylase.
abstract: This paper describes phosphorylase-catalyzed enzymatic alpha-glucosaminylation for the direct incorporation of a 2-amino-2-deoxy-alpha-D-glucopyranose unit into maltooligosaccharides. When the reaction of 2-amino-2-deoxy-alpha-D-glucopyranosyl 1-phosphate as the glycosyl donor with maltotetraose as a glycosyl acceptor was performed in the presence of phosphorylase, glucosaminylated oligosaccharides were produced, which were characterized by MALDI-TOF MS measurement after N-acetylation of the crude products. The N-acetylated derivative of the main product in this system was isolated by using HPLC, and its structure was confirmed by MS and (1)H NMR spectra. Furthermore, glucoamylase-catalyzed reaction of the isolated compound provided support that the alpha-glucosamine unit is positioned at the non-reducing end of the oligosaccharide.
authors.affiliation: Department of Nanostructured and Advanced Materials, Graduate School of Science and Engineering, Kagoshima University, 1-21-40 Korimoto, Kagoshima 890-0065, Japan.
authors.forename: Mutsuki
authors.initials: M
authors.lastname: Nawaji
authors.forename: Hironori
authors.initials: H
authors.lastname: Izawa
authors.forename: Yoshiro
authors.initials: Y
authors.lastname: Kaneko
authors.forename: Jun-Ichi
authors.initials: J
authors.lastname: Kadokawa