Yoshinaga Kazuhiro, Abe Jun-ichi, Tanimoto Toshiko, Koizumi Kyoko, Hizukuri Susumu
The United Graduate School of Agricultural Sciences, Kagoshima University, Korimoto 1-21-4, Kagoshima 890-0065, Japan.
Carbohydr Res. 2003 Oct 10;338(21):2221-5. doi: 10.1016/s0008-6215(03)00341-0.
A novel disaccharide, glucosyl 1,5-anhydro-D-fructose (1,5-anhydro-3-O-alpha-glucopyranosyl-D-fructose, GAF) was enzymatically prepared from 1,5-anhydro-D-fructose (1,5-AF) and cyclomaltoheptaose (beta-cyclodextrin). Cyclodextrin glucanotransferase transferred various sizes of maltooligosaccharide to 1,5-AF. Glucoamylase digested the maltooligosyl chain of the products to a glucosyl residue giving a final product, GAF. An NMR analysis of GAF elucidated that the glucose residue was linked to C-3 of the 1,5-AF residue with an ether linkage. Reactivity on the aminocarbonyl reaction of GAF with bovine serum albumin was lower than that of 1,5-AF, but was higher than that of glucose.
一种新型二糖,葡萄糖基1,5-脱水-D-果糖(1,5-脱水-3-O-α-吡喃葡萄糖基-D-果糖,GAF)是由1,5-脱水-D-果糖(1,5-AF)和环麦芽七糖(β-环糊精)酶法制备而成。环糊精葡糖基转移酶将不同大小的麦芽寡糖转移至1,5-AF上。葡糖淀粉酶将产物的麦芽寡糖链消化为一个葡萄糖残基,从而得到最终产物GAF。对GAF的核磁共振分析表明,葡萄糖残基通过醚键与1,5-AF残基的C-3相连。GAF与牛血清白蛋白的氨基羰基反应活性低于1,5-AF,但高于葡萄糖。