Binding of curcumin to milk proteins increases after static high pressure treatment of skim milk
Articolo
Data di Pubblicazione:
2013
Citazione:
Binding of curcumin to milk proteins increases after static high pressure treatment of skim milk / S. Rahimi Yazdi, F. Bonomi, S. Iametti, M. Miriani, A. Brutti, M. Corredig. - In: THE JOURNAL OF DAIRY RESEARCH. - ISSN 0022-0299. - 80:2(2013 May), pp. 152-158. [10.1017/S0022029913000125]
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.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
Curcumin ; milk proteins ; steady-state fluorescence ; fluorescence quenching ; high hydrostatic pressure
Elenco autori:
S. Rahimi Yazdi, F. Bonomi, S. Iametti, M. Miriani, A. Brutti, M. Corredig
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