Morimoto Kenji, Yoshihara Akihide, Furumoto Toshio, Takata Goro
Rare Sugar Research Center, Kagawa University, Miki-cho, Kagawa 761-0795, Japan.
Rare Sugar Research Center, Kagawa University, Miki-cho, Kagawa 761-0795, Japan.
J Biosci Bioeng. 2015 Jun;119(6):652-6. doi: 10.1016/j.jbiosc.2014.11.011. Epub 2014 Dec 8.
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.
来自肠系膜明串珠菌的蔗糖磷酸化酶（SPase）对8种己酮糖（表现为D-葡萄糖基受体）和α-D-葡萄糖-1-磷酸（G1P，表现为供体）具有活性。随后，所有这8种己酮糖都被转化为相应的D-葡萄糖基-己酮糖。在本研究评估的8种己酮糖中，D-阿洛酮糖是SPase的最佳底物，所得的D-葡萄糖基-D-阿洛酮糖苷产物是一种比旋光度为[α]D(20) + 74.36°的非还原糖。通过核磁共振分析，D-葡萄糖基-D-阿洛酮糖苷被鉴定为α-D-吡喃葡萄糖基-(1→2)-β-D-阿洛呋喃糖苷。D-葡萄糖基-D-阿洛酮糖苷对酵母转化酶表现出抑制活性，其Km值为50 mM，表现为竞争性抑制剂，Ki值为9.2 mM。还使用SPase和D-塔格糖3-表异构酶从蔗糖成功制备了D-葡萄糖基-D-阿洛酮糖苷。该过程还能从蔗糖中产生G1P，从D-果糖中产生D-阿洛酮糖，这表明该方法可用于制备D-葡萄糖基-D-阿洛酮糖苷，而无需使用诸如G1P和D-阿洛酮糖等昂贵试剂。
