Heating of milk alters the binding of curcumin to casein micelles. A fluorescence spectroscopy study

Food Chemistry

Volumn 132, Issue 3, 2012, Pages 1143-1149

  Rahimi Yazdi, S ^a   Corredig, M ^a  

^a UNIVERSITY OF GUELPH   (Canada)

Author keywords

Casein micelles; Curcumin; Fluorescence quenching; Protein polyphenol interactions; Steady state fluorescence; Whey proteins

Indexed keywords

CASEIN MICELLES; CURCUMIN; FLUORESCENCE QUENCHING; STEADY-STATE FLUORESCENCE; WHEY PROTEINS;

AMINO ACIDS; CASEIN; CENTRIFUGATION; FLUORESCENCE; FLUORESCENCE SPECTROSCOPY; HEATING; HYDROPHOBICITY; MICELLES; QUENCHING;

PROTEINS;

CASEIN; CURCUMIN; MILK PROTEIN; TRYPTOPHAN;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; FLUORESCENCE SPECTROSCOPY; HEATING; HYDROPHOBICITY; MICELLE; MILK; PROTEIN BINDING; PROTEIN DENATURATION; STEADY STATE; SURFACE PROPERTY;

CURCUMA LONGA;

EID: 84856220538     PISSN: 03088146     EISSN: 18737072     Source Type: Journal    
DOI: 10.1016/j.foodchem.2011.11.019     Document Type: Article

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