Gamma/alpha‐zein hydrolysates as oral delivery vehicles: Enhanced physicochemical stability and in vitro bioaccessibility of curcumin

Abstract

Summary In this study, we aimed to evaluate the potential of the γ‐zein hydrolysate (γ‐ZH) as a new delivery system for hydrophobic bioactive molecules such as curcumin (Cur). γ‐ZH‐Cur complexes (γ‐ZH‐Cur) with a particle size of 50–60 nm were successfully formed via the hydrogen bonding and hydrophobic interactions. Compared to α‐ZH, the complexation of Cur in γ‐ZH showed a better improvement in the water solubility and physicochemical stability of Cur and showed sustained release and greater potential for absorption of Cur. The differences in the loading capability, the physicochemical storage and the bioaccessibility of Cur between γ‐ZH and α‐ZH may be associated with the differences in the amino acid composition and typical sequence of peptides. These results indicate that γ‐ZH has a better ability to serve as a novel delivery for the hydrophobic bioactive molecules compared to α‐ZH.

Interaction of Soy Protein Isolate Hydrolysates with Cyanidin-3-O-Glucoside and Its Effect on the In Vitro Antioxidant Capacity of the Complexes under Neutral Condition

“…In novel beverages containing protein hydrolysates and polyphenols, it is possible that peptides and polyphenols interact, but only a few researchers have focused on these types of interactions [ 11 ]. Previous studies have found that curcumin delivery vehicles constructed with soy protein hydrolysates or γ-zein hydrolysates enhanced sustained release, encapsulation efficiency, and physicochemical stability of curcumin [ 12 , 13 ]. In one study, Milea et al [ 14 ] improved the functional properties of flavonoids extracted from yellow onion skins through freeze-drying microencapsulation that was obtained with whey protein hydrolysates and different polymer-based coating materials.…”

Expanding the Scope of Polyoxometalates as Artificial Proteases towards Hydrolysis of Insoluble Proteins

“…The commercially available zein used in this study mostly contains the α‐subunit with a significant amount of Tyr residues (approximately 5 wt %), which have a fluorescence emission maximum around 304 nm, while the amount of Trp and Phe residues is negligible [44] . However, as observed from the presence of additional bands in the SDS‐PAGE (Figure 3) commercially available zein may contain other variations of zein, such as the β‐subunit, which was observed as a weak band at around 16 kDa on the SDS‐PAGE gel, and may contain Trp residues which have a higher absorptivity and slightly higher quantum yield [45,46] . The interactions of Zr‐K 1 : 2 with zein were studied by following the quenching of the fluorescence emission of zein with increasing amounts of Zr‐K 1 : 2.…”

Expanding the Scope of Polyoxometalates as Artificial Proteases towards Hydrolysis of Insoluble Proteins

“…[44] However, as observed from the presence of additional bands in the SDS PAGE (Figure 3) commercially available zein may contain other variations of zein, such as the β-subunit which was observed as a weak band at around 16 kDa on the SDS PAGE gel, and may contain Trp residues which have a higher absorptivity and slightly higher quantum yield than Tyr. [45,46] The interactions of Zr-K 1:2 with zein were studied by following the quenching of the fluorescence emission of zein with increasing amounts of Zr-K 1:2. The binding strength, determined from the association constant (Ka), and the number of binding molecules (n) involved in the interaction leading to quenching can be calculated via the derived Stern-Volmer (SV) equation:…”