Main content area

Complexation of curcumin with Lepidium sativum protein hydrolysate as a novel curcumin delivery system

Kadam, Deepak, Palamthodi, Shanooba, Lele, S.S.
Food chemistry 2019 v.298 pp. 125091
Lepidium sativum, antioxidant activity, bioactive compounds, bioavailability, curcumin, dietary protein, emulsions, fluorescence emission spectroscopy, functional foods, hydrophobic bonding, in vitro digestion, intestines, lipophilicity, pH, protein hydrolysates, solubility
The complexation of Lepidium sativum protein hydrolysate (LSPH) with a lipophilic molecule, curcumin (CUR), and its effect on curcumin in vitro bioaccessibility/stability, functional and antioxidant activity were investigated. Fluorescence spectroscopy of the LSPH/CUR complex confirmed the presence of hydrophobic interactions that led to the complex formation. The LSPH (10–30 kDa) fraction showed a compact complexation with curcumin at pH 3.0 with excellent aqueous solubility, stability, and bioaccessibility. Further, complexation enhanced the aqueous solubility of curcumin more than 856-fold. In vitro sequential simulated gastric and intestinal digestion indicated that the bioaccessibility of curcumin was increased from 67% to 95% post complexation. The functional attributes suggest that the LSPH/CUR complex has good foam-forming capacity and emulsion stability, which are crucial for food product formulations. The results indicate that, since LSPH is a dietary protein, it might possibly be formulated as a functional food and as an excellent lipophilic bioactive molecule delivery vehicle in food formulations.