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Interaction of rS1-Casein with Curcumin and Its Biological Implications

Sneharani, A. H. and Sridevi Annapurna, Singh and Appu Rao, A. G. (2009) Interaction of rS1-Casein with Curcumin and Its Biological Implications. Journal of Agricultural Food and Chemistry, 57. pp. 10386-10391.

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RS1-Casein is one of the major protein components of the casein fraction of milk. Curcumin (diferuloyl methane), the major curcuminoid, constituting about 2-5% of turmeric (Curcuma longa) is the active ingredient with many physiological, biochemical, and pharmacological properties. On the basis of spectroscopic measurements, it is inferred that curcumin binds to RS1-casein at pH 7.4 and 27 �C with two binding sites, one with high affinity [(2.01 ( 0.6) � 106 M-1] and the other with low affinity [(6.3 ( 0.4) � 104 M-1]. Binding of curcumin to RS1-casein is predominantly hydrophobic in nature. The anisotropy of curcumin or conformation of RS1-casein did not change on interaction. The stability of curcumin in solution at pH 7.2 was enhanced on binding with RS1-casein. The chaperone-like activity of RS1-casein gets slightly enhanced on its binding to curcumin. The ability of curcumin to protect erythrocytes against hemolysis was not affected due to curcumin- RS1-casein interaction. The two binding sites of RS1-casein for curcumin, along with enhanced solution stability on interaction, may offer an alternative approach in physiological and nutritional applications.

Item Type: Article
Uncontrolled Keywords: RS1-Casein; curcumin stability; fluorescence titration; circular dichroism; chaperone activity
Subjects: 500 Natural Sciences and Mathematics > 10 Plants
600 Technology > 08 Food technology > 16 Nutritive value > 03 Proteins
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 08 Jun 2009 06:56
Last Modified: 04 Sep 2018 11:35
URI: http://ir.cftri.com/id/eprint/9015

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