2015
DOI: 10.1016/j.foodhyd.2014.12.008
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Evaluation of structural and functional properties of protein–EGCG complexes and their ability of stabilizing a model β-carotene emulsion

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Cited by 228 publications
(115 citation statements)
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“…Thus, it is reasonable to conclude that the collective effect of HSPI and rutin plays a role in interfacial adsorption, promoting the complex migration to the oil–water interface. In this respect, Wei and others () have shown that protein–EGCG complexes exhibited better interfacial adsorption behavior and greater antioxidant potential in emulsion systems. Based on diffusion‐controlled adsorption process, the diffusion rate ( k diff ) was also calculated in the initial (<300 s) of π increase (Figure A) and the changes in k diff among various samples are consistent with π 0 value (Table ).…”
Section: Resultsmentioning
confidence: 94%
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“…Thus, it is reasonable to conclude that the collective effect of HSPI and rutin plays a role in interfacial adsorption, promoting the complex migration to the oil–water interface. In this respect, Wei and others () have shown that protein–EGCG complexes exhibited better interfacial adsorption behavior and greater antioxidant potential in emulsion systems. Based on diffusion‐controlled adsorption process, the diffusion rate ( k diff ) was also calculated in the initial (<300 s) of π increase (Figure A) and the changes in k diff among various samples are consistent with π 0 value (Table ).…”
Section: Resultsmentioning
confidence: 94%
“…In fact, most researchers have prepared protein‐based emulsions by directly introducing hydrophobic polyphenols using protein as a carrier followed by homogenization procedure (Atarés and others ; Cui and others ). The incorporation of polyphenols into protein to form a cranberry polyphenol–protein complex has been used to promote oxidative stability of protein emulsions (Wan and others ; Wei and others ). However, more likely, direct mixing may cause the deficiency of antioxidant effectiveness due to the inefficient binding capacity of native protein to polyphenols (Shpigelman and others ; Atarés and others ).…”
Section: Introductionmentioning
confidence: 99%
“…investigated the covalent modification of protein by EGCG and observed the binding of EGCG to thiol group of cysteine in the protein chain to form an S ‐cysteinyl‐EGCG adduct . A recent study demonstrated the attachment of EGCG to whey proteins including α‐lactalbumin and β‐lactoglobulin under alkaline conditions, subsequently causing the formation of EGCG–protein conjugates . According to these results in the literature, it was often accepted that modification products were EGCG–protein adducts.…”
Section: Resultsmentioning
confidence: 99%
“…Epigallocatechin gallate (EGCG) is the most abundant and biologically active polyphenol in green tea [16], and recent studies have shown that EGCG can interact with many proteins including β-lactoglobulin, and human serum albumin by formation of non-covalent or covalent bonds [5,17,18]. Results also suggest that these reactions can change the net charge of the protein molecules, which may affect their solubility and subsequent digestion by gastrointestinal enzymes [1,19].…”
Section: Introductionmentioning
confidence: 99%