Synthesis of ECG ((−)-epicatechin gallate) acylated derivatives as new inhibitors of α-amylase and their mechanism on delaying starch digestion. (April 2023)

• Record Type: Journal Article
• Authors: Wang, Shan; Jiang, Chao; Jing, Huijuan; Du, Xiaojing; Zhu, Song; Wang, Hongxin; Ma, Chaoyang
• Is Part Of: Food bioscience. Volume 52(2023)
• Publication Date: 2023-04
• Subjects: ECG derivatives -- α-Amylase -- Fluorescence quenching -- Molecular docking -- Simulated digestion; Food -- Biotechnology -- Periodicals; Food -- Research -- Periodicals; Aliments -- Biotecnologia -- Revistes; Aliments -- Investigació -- Revistes; Food -- Biotechnology; Food -- Research; Revistes electròniques; Periodicals; 664.005
• DOI: 10.1016/j.fbio.2023.102466
• Languages: English
• ISSNs: 2212-4292

Abstract

Abstract: (−)-Epicatechin gallate (ECG), as a natural α-amylase inhibitor, has received extensive attention. However, poor liposolubility of ECG limits its application. In this study, lipophilic derivatives of ECG (1A-ECG, 2A-ECG, 1B-ECG, and 2B-ECG) were synthesized by Lipozyme TLIM ( Thennomyces lanuginosus ) and their mechanism on delaying starch digestion was investigated. The results showed that the conversion of ECG exceeded 70% under optimal conditions. Interestingly, compared with ECG, the inhibitory activities of ECG derivatives on α-amylase decreased, while the inhibitory activity of 1A-ECG on α-amylase increased. Though the main force between ECG and 1A-ECG with α-amylase was induced by hydrogen bond, hydrophobic interaction was the main force between other derivatives with α-amylase. However, the addition of four ECG derivatives can effectively reduce the proportion of rapidly digestible starch, and delay the digestion of starch. This study may expand the applications of ECG and provide a theoretical basis for 1A-ECG to delay the digestion of starch. Graphical abstract: Image 1 Highlights: (−)-Epicatechin gallate (ECG) derivatives were synthesized. 1A-ECG possessed superior inhibitory actions on α-amylase than ECG. The main interactive force of 1A-ECG on α-amylase was hydrogen bond. Larger molecular size of ECG derivatives prevents their combination with α-amylase. Four ECG derivatives would convert more RDS to RS than ECG.