Enzymatic synthesis of glucosyl-sugar alcohols using various transglycosylating enzymes, such as cyclodextrin glucanotransferase (CGTase), ${alpha}$-amylase, ${alpha}$-glucosidase, and pullulanase was investigated using various sugar alcohols, such as sorbitol, xylitol, inositol, maltitol, and lactitol as glucosyl acceptors. CGTase showed the highest transglycosylating activity to sugar alcohols compared to other transglycosylating enzymes, and inositol and maltitol were the most suitable glucosyl acceptors. Soluble starch, extruded starch, cyclodextrins, and maltooligosaccharides were also identified to be adequate glucosyl donors for transglycosylation reaction of CGTase to sugar alcohols. The synthesis of glucosyl-maltitol in the reaction system using extruded starch as the glucosyl donor and maltitol as the glucosyl acceptor showed the best results showing the highest transglycosylation yield. The transglycosylation products were purified by activated carbon column chromatography with ethanol gradient elution. Chemical structures of above transglucosylated products were analyzed by nuclear magnetic resonance spectroscopy, and two products were identified to be maltotritol and maltotetraitol, in which one or two glucose molecules attached to the parent maltitol molecule by a ${alpha}$-l,4-glucosidic bond, respectively.