Maltosyl-erythritol, a Major Transglycosylation Product of Erythritol byBacillus stearothermophilusMaltogenic Amylase

Abstract

This study was done to modify erythritol to change its physicochemical and sensory properties. Erythritol, a four-carbon sugar alcohol, was transglycosylated by Bacillus stearothermophilus maltogenic amylase with maltotriose as a donor molecule. The presence of various transglycosylation products of erythritol was confirmed by TLC and high performance ion exchange chromatography (HPIC). The major transfer product was purified by gel filtration chromatography on Bio-Gel P-2. Examination by LC-MS, matrix-assisted laser desorption ionisation-time of flight mass spectrometry (MALDI-TOF-MS), and 13C NMR showed that the major transfer product was maltosyl-erythritol. Results of 13C NMR of maltosyl-erythritol suggested that linkage was formed between the C1 carbon of glucose unit in maltose and either one of the two carbon atoms of the terminal hydroxyl groups of erythritol, so that a mixture of 1-O- and 4-O-alpha-maltosyl-erythritol was produced. The sweetness of maltosyl-erythritol was about 40% that of sucrose, and its negative sensory properties were less than those of erythritol.

Characterization and gene cloning of a maltotriose-forming exo-amylase from Kitasatospora sp. MK-1785

“…For example, it was reported that a maltotrioseforming amylase from Streptomyces griseus and a maltotetraose-forming amylase from Pseudomonas stutzeri could transfer maltotriose and maltotetraose to p-nitrophenyl α-glucopyranoside, respectively (Usui and Murata 1988;Usui et al 1993). Furthermore, a maltogenic amylase from Geobacillus stearothermophilus recognized not only saccharides, but also sugar alcohols and ascorbic acid, as maltose acceptors in transglycosylation reaction Roh et al 2005;Yoon et al 2003;Bae et al 2002). Thus, exo-α-amylases are also useful for maltooligosaccharideglycoside synthesis.…”

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2003–2004

“…β-galactosidase from Bacillus circulans TOF (DHB) (Farkas, et al, 2003) , et al, 2004d) β-D-Glucosamine-containing nonasaccharide Chemical synthesis with isopropyl thioglycosides TOF (CHCA) β-D-Glucosamine-containing oligosaccharides Chemical synthesis with isopropyl thioglycosides TOF (CHCA) (Yang, Hua & Du, 2003) Glucosylated isokestose and nystose Enzymatic (kojibiose phosphorylase from Thermoanaerobacter brockii to synthesise five novel oligosaccharides TOF Glycosaminotrioses With GalNAc or ManNAc termini. To study binding to hevein from Hevea braziliensis TOF (CHCA) (Aboitiz, et al, 2004) Imino sugar scaffolds For the generation of glycosidase inhibitor libraries TOF (DHB) (La Ferla, et al, 2004) Kanamycin analogues Chemical synthesis and antibacterial evaluation MALDI (Li, et al, 2004b) Lacto-N-neotetraose Dendrimeric polyethylene glycol supported synthesis TOF (CHCA) (He, Gu & Du, 2003) Lepidimoide Unsaturated disaccharide (4-deoxy-β-L-threo-hex-4enopyranosyl-(1→2)-L-Rhap) from okra mucilage TOF (Co powder) (Manzoni & Castelli, 2004) Maltooligosyl fructofuranosides Immobilized cyclodextrin glucosyltransferase catalyst TOF (DHB) Maltosyl-erythritol Transglycosylation product of erythritol by maltogenic amylase TOF (CHCA) (Yoon, et al, 2003) α-(1→3)-linked manno-hexaose and -octaose α-(1-3)-linked di-and tetra-saccharide donor + tetrasaccharide TOF (Chen & Kong, 2002) Mannosides Synthesis by double differential glycosylation by lanthanide triflates TOF i , et al, 2004) 4-O-Me-maltosyl fluoride plus gluconohydroxoximino-1,5-lactam…”

“…TOF (CHCA) Glycolipids with partially F-alkyl chains For study of lipid monolayers TOF (DHB) (Gege, et al, 2004 (Stadelmaier, et al, 2003) Maltosyl erythritol Transglycosylation with amylase (Bacillus stearothermophilus) TOF (CHCA) (Yoon, et al, 2003) 6-O-Sulfo Lewis X neo-glycolipid Containing lactamized neuraminic acid TOF (DHB) Cyclodextrins Acetylated α, β and γ cyclodextrins Chemical synthesis. Properties in dense CO 2 TOF (Potluri, et al, 2003) Allylated cyclodextrin…”

Molecular Cloning and Enzymatic Characterization of Cyclomaltodextrinase from Hyperthermophilic Archaeon Thermococcus sp. CL1

“…These three enzymes are almost equivalent in terms of their catalytic properties and threedimensional structures [12]. They not only show hydrolyzing activity on CDs and other carbohydrate substrates, including pullulan and soluble starch, but also perform transglycosylation reactions using various biological materials as acceptors [17,22,30]. In biological systems, CDase is suggested to be involved in the degradation of maltodextrin and glycogen in Bacillus subtilis, together with pullulanase [25].…”