Journal
FOOD CHEMISTRY
Volume 268, Issue -, Pages 334-341Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2018.06.015
Keywords
Milk protein; Phenol binding ability; Chlorogenic acid; Structure; Foaming properties; In vitro digestion; Fluorescence
Funding
- National Key Research and Development Program of China [2016YFD0401404]
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The effects of the interaction of whey protein isolate (WPI) and casein (CS) with chlorogenic acid (CA; 20, 120 and 240 mu mol/g protein) on the structural and functional properties of proteins were investigated. CA induced significant structural changes, increased digestibility, and improved functionalities of CS and WPI. Non-covalent association between CA and treated proteins was detected using Fourier transform infrared spectroscopy (FTIR), intrinsic tryptophan fluorescence, and ANS-augmented fluorescence. The CA binding affinity for WPI was superior to that for CS as indicated by higher K-sv. and lower hydrophobicity. Total sulfhydryl content in CS and WPI decreased, respectively, from 5.4 to 3.2 mu mol/g and from 21 to 7.8 mu mol/g, and surface hydrophobicity declined by 16.6% and 22.4% with 240 mu mol/g CA. Enhanced solubility and foaming capacity of the protein-phenol complex were demonstrated. CA at medium and high concentrations displayed a remarkable synergism of radical scavenging activity with peptides in both protein digests.
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