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

Abstract:

:The binding interactions between young apple polyphenols and porcine pancreatic α-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 α-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 α-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.

journal_name

Food Chem

journal_title

Food chemistry

authors

Sun L,Warren FJ,Gidley MJ,Guo Y,Miao M

doi

10.1016/j.foodchem.2019.01.087

subject

Has Abstract

pub_date

2019-06-15 00:00:00

pages

468-474

eissn

0308-8146

issn

1873-7072

pii

S0308-8146(19)30155-4

journal_volume

283

pub_type

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