期刊
FOOD CHEMISTRY
卷 168, 期 -, 页码 276-287出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2014.07.056
关键词
Green coffee; beta-Cyclodextrin; Protein-polyphenol interactions; Liquid chromatography-tandem mass; spectrometry; Molecular modelling
资金
- National Center of Science [UMO-2011/03/B/NZ9/00745]
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 beta-cyclodextrin strongly limited these interactions to a level of 0.03-0.06 g/100 g. (C) 2014 Elsevier Ltd. All rights reserved.
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