邻苯三酚
化学
烘烤
二聚体
IC50型
多酚
阿卡波糖
非竞争性抑制
非竞争性抑制剂
立体化学
生物化学
有机化学
酶
抗氧化剂
体外
物理化学
作者
Hui Wang,Xiaoli Kang,Shiwei Sun,Yichen Yin,Kun Jiang,Guodong Tang,Xinning Tang,Wei Wang
标识
DOI:10.1016/j.fbio.2022.101583
摘要
The roasting process of pyrogallol, a polyphenol compound distributed in coffee beverages, significantly enhanced its α-glucosidase inhibitory activity. In this study, a bioassay-guided isolation of the thermal reaction products of pyrogallol led to the identification of two potent α-glucosidase inhibitors, 4-4′ dimer of pyrogallol (4,4′-DP) and 4-5′ dimer of pyrogallol (4,5′-DP). Their α-glucosidase inhibitory activity was higher than that of pyrogallol, as evidenced by comparing the IC50 values (206.2 ± 1.2 μM for 4,4′-DP, 187.6 ± 2.6 μM for 4,5′-DP, 2660 ± 60.1 μM for pyrogallol). And the roasting products were more potent α-glucosidase inhibitors compared to acarbose (IC50 = 695 ± 12.7 μM). Enzyme kinetics demonstrated that 4,4′-DP and 4,5′-DP inhibited α-glucosidase in an uncompetitive and a non-competitive manner, respectively. Docking simulations revealed that the main interaction forces between these two compounds and α-glucosidase were hydrogen bonding and hydrophobic effect. These results suggested that a simple roasting process might increase the α-glucosidase inhibitory activity of pyrogallol-containing foods such as coffee beverages.
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