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Binding of curcumin to milk proteins increases after static high pressure treatment of skim milk

Published online by Cambridge University Press:  03 April 2013

Saeed Rahimi Yazdi ,
Francesco Bonomi ,
Stefania Iametti ,
Matteo Miriani ,
Andrea Brutti  and
Milena Corredig
Saeed Rahimi Yazdi
Affiliation:
Department of Food Science, University of Guelph, Guelph, Ontario N1H 2W1, Canada
Francesco Bonomi
Affiliation:
Section of Chemical and Biomolecular Sciences, DeFENS, University of Milan, 20122 Milano, Italy
Stefania Iametti
Affiliation:
Section of Chemical and Biomolecular Sciences, DeFENS, University of Milan, 20122 Milano, Italy
Matteo Miriani
Affiliation:
Section of Chemical and Biomolecular Sciences, DeFENS, University of Milan, 20122 Milano, Italy
Andrea Brutti
Affiliation:
Experimental Station for the Food Preserving Industry (SSICA), 43100 Parma, Italy
Milena Corredig*
Affiliation:
Department of Food Science, University of Guelph, Guelph, Ontario N1H 2W1, Canada
*
*For correspondence; e-mail: [email protected]
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Abstract

Curcumin is a bioactive polyphenolic compound extracted from turmeric with known anti-inflammatory properties, and its hydrophobic nature restricts its solubility and its bioaccessibility. Solubility may be improved upon binding of curcumin to native or treatment-modified casein micelles. The present work demonstrated that high hydrostatic pressure treatment of skim milk increases the binding of curcumin to caseins. The association of curcumin to casein micelles was assessed using fluorescence spectroscopy, either directly or by tryptophan quenching. The amount of curcumin associated with the milk proteins increased in pressure-treated milk, and a further improvement in the amount of bound curcumin was observed upon pressure treatment of a milk/curcumin mixture. However, in this case, some of the curcumin dissociated during storage, contrarily to what was observed for untreated milk. From a molecular standpoint, the data presented here indicate that structural modifications induced by high-pressure treatment and known to affect the structure of milk proteins result in a rearrangement of the amino acid residues in close proximity to the protein-associated curcumin.

Keywords

Curcuminmilk proteinssteady-state fluorescencefluorescence quenchinghigh hydrostatic pressure
Type
Research Article
Information
Journal of Dairy Research , Volume 80 , Issue 2 , May 2013 , pp. 152 - 158
Copyright
Copyright © Proprietors of Journal of Dairy Research 2013

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