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

被引:75
作者
Budryn, Grazyna [1 ]
Palecz, Bartlomiej [2 ]
Rachwal-Rosiak, Danuta [1 ]
Oracz, Joanna [1 ]
Zaczynska, Donata [1 ]
Belica, Sylwia [2 ]
Navarro-Gonzalez, Inmaculada [3 ]
Vegara Meseguer, Josefina Maria [4 ]
Perez-Sanchez, Horacio [4 ]
机构
[1] Lodz Univ Technol, Fac Biotechnol & Food Sci, Inst Chem Food Technol, PL-90924 Lodz, Poland
[2] Univ Lodz, Fac Chem, Dept Phys Chem, PL-90131 Lodz, Poland
[3] Univ Murcia, Fac Vet Sci, Dept Food Sci & Nutr, Murcia, Spain
[4] Univ Catolica San Antonio Murcia UCAM, Dept Comp Sci, Bioinformat & High Performance Comp Res Grp BIO H, Murcia, Spain
关键词
Green coffee; beta-Cyclodextrin; Protein-polyphenol interactions; Liquid chromatography-tandem mass; spectrometry; Molecular modelling; BINDING; CHROMATOGRAPHY; STABILITY; PHENOLICS; AFFINITY; RELEASE; MODEL; PH;
D O I
10.1016/j.foodchem.2014.07.056
中图分类号
O69 [应用化学];
学科分类号
070301 [无机化学];
摘要
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.
引用
收藏
页码:276 / 287
页数:12
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