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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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Abstract
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.res.in/id/eprint/9015 |
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