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

Grażyna Budryn; Bartłomiej Pałecz; Danuta Rachwał-Rosiak; Joanna Oracz; Donata Zaczyńska; Sylwia Belica; Inmaculada Navarro-González; Josefina María Vegara Meseguer; Horacio Pérez-Sánchez

doi:10.1016/j.foodchem.2014.07.056

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

Food Chem. 2015 Feb 1:168:276-87. doi: 10.1016/j.foodchem.2014.07.056. Epub 2014 Jul 15.

Authors

Grażyna Budryn¹, Bartłomiej Pałecz², Danuta Rachwał-Rosiak³, Joanna Oracz³, Donata Zaczyńska³, Sylwia Belica², Inmaculada Navarro-González⁴, Josefina María Vegara Meseguer⁵, Horacio Pérez-Sánchez⁶

Affiliations

¹ Institute of Chemical Food Technology, Faculty of Biotechnology and Food Sciences, Lodz University of Technology, 90-924 Lodz, Poland. Electronic address: grazyna.budryn@p.lodz.pl.
² Departments of Physical Chemistry, Faculty of Chemistry, University of Lodz, 90-131 Lodz, Poland.
³ Institute of Chemical Food Technology, Faculty of Biotechnology and Food Sciences, Lodz University of Technology, 90-924 Lodz, Poland.
⁴ Department of Food Science and Nutrition, Faculty of Veterinary Science, University of Murcia, Campus de Espinardo, Regional Campus of International Excellence "Campus Mare Nostrum", Murcia, Spain.
⁵ Bioinformatics and High Performance Computing Research Group (BIO-HPC), Computer Science Department, Universidad Católica San Antonio de Murcia (UCAM), Guadalupe, Murcia, Spain.
⁶ Bioinformatics and High Performance Computing Research Group (BIO-HPC), Computer Science Department, Universidad Católica San Antonio de Murcia (UCAM), Guadalupe, Murcia, Spain. Electronic address: hperez@ucam.edu.

PMID: 25172711
DOI: 10.1016/j.foodchem.2014.07.056

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 12.1-14.4g/100g 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 0.33-2.67g/100g. Inclusion of CHAs with β-cyclodextrin strongly limited these interactions to a level of 0.03-0.06g/100g.

Keywords: Green coffee; Liquid chromatography–tandem mass spectrometry; Molecular modelling; Protein–polyphenol interactions; β-Cyclodextrin.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Chlorogenic Acid / chemistry*
Coffee / chemistry*
Coumaric Acids / chemistry*
Egg Proteins / chemistry*
Models, Molecular
Soybean Proteins / chemistry*
Tandem Mass Spectrometry / methods
Whey Proteins / chemistry*

Substances

Coffee
Coumaric Acids
Egg Proteins
Soybean Proteins
Whey Proteins
Chlorogenic Acid