Inhibitory potential of phenolic compounds of Thai colored rice (Oryza sativa L.) against α‐glucosidase and α‐amylase through in vitro and in silico studies

香兰素酸 丁香酸 水稻 化学 淀粉酶 食品科学 生物化学 抗氧化剂 没食子酸 基因
作者
Sompong Sansenya,Apirak Payaka
出处
期刊:Journal of the Science of Food and Agriculture [Wiley]
卷期号:102 (14): 6718-6726 被引量:6
标识
DOI:10.1002/jsfa.12039
摘要

This study investigated the inhibitory efficiency of phenolic compounds content methyl vanillate, syringic acid and vanillic acid against α-glucosidase and α-amylase. The phenolic compound contents of 10 Thai colored rice cultivars were also determined, and the relationship between the inhibitory efficiency of colored rice extract with methyl vanillate, syringic acid and vanillic acid was evaluated.The results revealed that the inhibition efficiency of methyl vanillate, syringic acid and vanillic acid was higher against α-glucosidase than against α-amylase. Inhibitory activity of vanillic acid against α-glucosidase and α-amylase was highest, with IC50 of 0.100 ± 0.01 and 0.130 ± 0.02 mmol L-1 , respectively. Docking study showed strong binding by three hydrogen bonds and four hydrogen bonds between vanillic acid with the amino acid in the binding site of α-glucosidase and α-amylase, respectively. Inhibition modes of these phenolic compounds were defined as a mixed type inhibition against α-glucosidase. Highest phenolic compound contents of methyl vanillate, syringic acid and vanillic acid were obtained from methanol extracts of all rice cultivars. The methanol extracts of all colored rice cultivars such as Khao Leum Pua also showed the highest inhibition potential against α-glucosidase and α-amylase. The results indicated that these phenolic compound contents were closely related to the inhibition potential of colored rice extracts against α-glucosidase and α-amylase.Our results suggest that rice, especially colored rice cultivars, has the source of phenolic compounds. Moreover, the phenolic compounds had the greatest source of natural inhibitor against α-glucosidase and α-amylase. © 2022 Society of Chemical Industry.
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