Mechanism of binding interactions between young apple polyphenols and porcine pancreatic α-amylase

被引：53

作者：

Sun, Lijun ^{[1
]}

Warren, Frederick J. ^{[3
]}

Gidley, Michael J. ^{[2
]}

Guo, Yurong ^{[5
]}

Miao, Ming ^{[4
]}

机构：

[1] Northwest A&F Univ, Coll Food Sci & Engn, Yangling, Shaanxi, Peoples R China

[2] Univ Queensland, Ctr Nutr & Food Sci, Queensland Alliance Agr & Food Innovat, St Lucia, Qld 4072, Australia

[3] Norwich Res Pk, Quadram Inst Biosci, Norwich NR4 7UA, Norfolk, England

[4] Jiangnan Univ, State Key Lab Food Sci & Technol, 1800 Lihu Ave, Wuxi 214122, Jiangsu, Peoples R China

[5] Shaanxi Normal Univ, Coll Food Engn & Nutr Sci, Xian 710062, Shaanxi, Peoples R China

来源：

FOOD CHEMISTRY | 2019年 / 283卷

基金：

英国生物技术与生命科学研究理事会; 国家重点研发计划;

关键词：

Young apple polyphenols; Porcine pancreatic alpha-amylase; Binding interactions; Inhibition; ISOTHERMAL TITRATION CALORIMETRY; DIETARY POLYPHENOLS; CHLOROGENIC ACID; GREEN TEA; INHIBITION; THEAFLAVINS; DIGESTION; KINETICS; AFFINITY; DSC;

D O I：

10.1016/j.foodchem.2019.01.087

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

The binding interactions between young apple polyphenols and porcine pancreatic alpha-amylase were investigated through isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC) and molecular docking. The results obtained were compared with those obtained through inhibition kinetics and fluorescence quenching. It was found that binding of tannic acid, chlorogenic acid, caffeic acid and epicatechin with alpha-amylase is an exothermal process, with the binding constants in the order of tannic acid > chlorogenic acid > caffeic acid > epicatechin. This is consistent with the orders of reciprocal of competitive inhibition constant and fluorescence quenching constant. The binding energy obtained through molecular docking showed the same order, except for epicatechin. These results are consistent with the inhibition of alpha-amylase being caused by the binding of the polyphenols with the enzyme. In addition, from the fluorescence quenching and DSC data, total polyphenols, tannic acid, chlorogenic acid and caffeic acid were found to partially unfold the enzyme structure.

引用

页码：468 / 474

页数：7

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