Title of article :
Effect of inclusion of hydroxycinnamic and chlorogenic acids from green coffee bean in β-cyclodextrin on their interactions with whey, egg white and soy protein isolates
Author/Authors :
Budryn، نويسنده , , Gra?yna and Pa?ecz، نويسنده , , Bart?omiej and Rachwa?-Rosiak، نويسنده , , Danuta and Oracz، نويسنده , , Joanna and Zaczy?ska، نويسنده , , Donata and Belica، نويسنده , , Sylwia and Navarro-Gonz?lez، نويسنده , , Inmaculada and Meseguer، نويسنده , , Josefina Mar?a Vegara and Pérez-S?nchez، نويسنده , , Horacio، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2015
Pages :
12
From page :
276
To page :
287
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 :
Green coffee , ?-Cyclodextrin , Protein–polyphenol interactions , Liquid chromatography–tandem mass spectrometry , molecular modelling
Journal title :
Food Chemistry
Serial Year :
2015
Journal title :
Food Chemistry
Record number :
1979270
Link To Document :
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