柚皮素
化学
葡萄糖苷
生物转化
酶动力学
生物化学
立体化学
活动站点
酶
类黄酮
医学
替代医学
病理
抗氧化剂
作者
Shiu Yeh Yu,Yun-Sang So,Changjin Lim,Chi Heung Cho,Sang-Gil Lee,Sang‐Ho Yoo,Cheon Seok Park,Sang‐Ho Yoo,Kyung Hyun Min,Dong-Ho Seo
标识
DOI:10.1016/j.foodchem.2024.139182
摘要
Amylosucrase (ASase) efficiently biosynthesizes α-glucoside using flavonoids as acceptor molecules and sucrose as a donor molecule. Here, ASase from Deinococcus wulumuqiensis (DwAS) biosynthesized more naringenin α-glucoside (NαG) with sucrose and naringenin as donor and acceptor molecules, respectively, than other ASases from Deinococcus sp. The biotransformation rate of DwAS to NαG was 21.3% compared to 7.1–16.2% for other ASases. Docking simulations showed that the active site of DwAS was more accessible to naringenin than those of others. The 217th valine in DwAS corresponded to the 221st isoleucine in Deinococcus geothermalis AS (DgAS), and the isoleucine possibly prevented naringenin from accessing the active site. The DwAS-V217I mutant had a significantly lower biosynthetic rate of NαG than DwAS. The kcat/Km value of DwAS with naringenin as the donor was significantly higher than that of DgAS and DwAS-V217I. In addition, NαG inhibited human intestinal α-glucosidase more efficiently than naringenin.
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