Interaction of α_S1-Casein with Curcumin and Its Biological Implications

Abstract

alpha(S1)-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 alpha(S1)-casein at pH 7.4 and 27 degrees C with two binding sites, one with high affinity [(2.01 +/- 0.6) x 10(6) M(-1)] and the other with low affinity [(6.3 +/- 0.4) x 10(4) M(-1)]. Binding of curcumin to alpha(S1)-casein is predominantly hydrophobic in nature. The anisotropy of curcumin or conformation of alpha(S1)-casein did not change on interaction. The stability of curcumin in solution at pH 7.2 was enhanced on binding with alpha(S1)-casein. The chaperone-like activity of alpha(S1)-casein gets slightly enhanced on its binding to curcumin. The ability of curcumin to protect erythrocytes against hemolysis was not affected due to curcumin- alpha(S1)-casein interaction. The two binding sites of alpha(S1)-casein for curcumin, along with enhanced solution stability on interaction, may offer an alternative approach in physiological and nutritional applications.

Nanocomplexation of soy protein isolate with curcumin: Influence of ultrasonic treatment

“…The observations are well in accordance with those of the previous works (Chen et al, 2015;Tapal & Tiku, 2012). Similar improvements of storage stability for curcumin have been confirmed for the other proteins, including serum albumins and milk proteins (Barik, Priyadarsni, & Mohan, 2003;Leung & Kee, 2009;Sneharani, Karakkat, Singh, & Rao, 2010;Sneharani, Singh, & Rao, 2009;Wang et al, 1997).…”

“…Thus, besides the number of hydrophobic sites, the hydrophobic nature (strong or weak) is also an important factor affecting the complexation with curcumin. This might be the principal reason causing the differences in capacity to bind curcumin between different types of proteins, e.g., α s1 -casein, casein micelle, β-lactoglobulin, and SPI (Bourassa, Kanakis, Pollissiou, & Tajmir-Riahi, 2010;Chen et al, 2015;Sahu et al, 2008;Sneharani et al, 2009Sneharani et al, , 2010.…”

Improving antioxidant and antimicrobial properties of curcumin by means of encapsulation in gelatin through electrohydrodynamic atomization

“…In this regard, complexation of curcumin with several proteins has been deeply studied. Barik, Priyadarsini, and Mohan (2003); Leung and Kee (2009) ;Sneharani, Singh, and Rao (2009) ;Tapal and Tiku (2012) studied the binding of curcumin to bovine serum albumin, a s1 -casein, b-lactoglobulin, soy protein isolate, and plasma proteins (human serum albumin and fibrinogen), respectively. All these authors revealed the ability of curcumin to bind to proteins, thus increasing curcumin solubility and stability in aqueous media.…”

Curcumin encapsulated in the complex of lysozyme/carboxymethylcellulose and implications for the antioxidant activity of curcumin

“…Among these, using natural biopolymers as carriers to load Cur has received increasing interest due to their safe, biodegradable and reproducible perspective (Pan, Tikekar, Wang, Avena-Bustillos & Nitin, 2015;Sneharani, Singh & Appu Rao, 2009). Complexes based on natural proteins and polysaccharides with electrostatic interactions, hydrophobic interactions, and hydrogen bonds are more superior carriers than proteins alone because polysaccharides can restrain the aggregation of proteins especially at the isoelectric point of the proteins McClements, 2006).…”