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

• Published in: Food chemistry 2019-11, Vol.298, p.125091-125091, Article 125091
• Main Authors: Kadam, Deepak, Palamthodi, Shanooba, Lele, S.S.
• Format: Article
• Language: English
• Subjects: Bioaccessibility/stability; Complexation; Curcumin; Protein hydrolysate
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2019.125091

•Lepidium sativum protein hydrolysate (LSPH)-based curcumin (CUR) complexation was successfully achieved.•The LPSH (10–30 kDa) complex exhibited a good colloidal stability at pH 3.0.•The aqueous solubility, stability and even bioaccessibility were significantly enhanced.•The LPSH (10–30 kDa) could be a potential strategy for a delivery system. 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.