Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7595142 | Food Chemistry | 2015 | 12 Pages |
Abstract
The aim of the study was to characterise the interactions of hydroxycinnamic and chlorogenic acids (CHAs) from green coffee, with isolates of proteins from egg white (EWP), whey (WPC) and soy (SPI), depending on pH and temperature. The binding degree was determined by liquid chromatography coupled to a diode array detector and an ultrahigh resolution hybrid quadruple-time-of-flight mass spectrometer with ESI source (LC-QTOF-MS/MS). As a result of binding, the concentration of CHAs in proteins ranged from 9.44-12.2, 11.8-13.1 and 12.1-14.4 g/100 g for SPI, WPC and EWP, respectively. Thermodynamic parameters of protein-ligand interactions were determined by isothermal titration calorimetry (ITC) and energetics of interactions at the atomic level by molecular modelling. The amount of CHAs released during proteolytic digestion was in the range 0.33-2.67 g/100 g. Inclusion of CHAs with β-cyclodextrin strongly limited these interactions to a level of 0.03-0.06 g/100 g.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Grażyna Budryn, BartÅomiej PaÅecz, Danuta RachwaÅ-Rosiak, Joanna Oracz, Donata ZaczyÅska, Sylwia Belica, Inmaculada Navarro-González, Josefina MarÃa Vegara Meseguer, Horacio Pérez-Sánchez,