Self-Assembled Micellar Nanoparticles by Enzymatic Hydrolysis of High-Density Lipoprotein for the Formation and Stability of High Internal Phase Emulsions

Abstract

In this study, the influence of pH on the conformational state of EHT, which was obtained from the enzymatic hydrolysis of trypsin, and the stabilizing properties of high internal phase emulsions have been demonstrated. Critical micelle concentration and transmission electron microscopy results exhibited the formation of micellar nanoparticles with mean diameters ranging from 108 to 1359.5 nm. The results of solubility, surface hydrophobicity, and conformations indicated that EHT tended to act as particulate emulsifiers at pH 3, 5, and 7, while at alkaline pH, it was more like a polymeric emulsifier, which could be proven by confocal laser scanning microscopy. The EHT at pH 7 exhibited better stabilizing properties than those at pH 9 and 11 as influenced by storage, temperature, and ionic strength. These findings might be of great importance for broadening the range of sustainable applications of amphiphilic peptides in foods and pharmaceuticals.

A Comprehensive Review of Self-Assembled Food Protein-Derived Multicomponent Peptides: From Forming Mechanism and Structural Diversity to Applications

“…Additionally, Liu et al found that EYPNs with various sizes and highly pH-dependent structures could act as an efficient particulate emulsifier to stabilize O/W high-internal-phase emulsions (Figure e). The compact adsorption of EYPNs could explain the outstanding stability at the interface and the formation of a three-dimensional network …”

“…The self-assembly of FPDMPs into micellar structures has been extensively reported. For example, The amphiphilic egg yolk peptides obtained from enzymatic hydrolysis of purified defatted egg yolk proteins can self-assemble into micellar nanostructures under aqueous conditions at the CMC of about 0.1 mg/mL. , The observed results were attributed to the increased abundance of hydrophilic amino acids, including glutamic acid (Glu), lysine (Lys), arginine (Arg), aspartic acid (Asp), and serine (Ser), in the amphiphilic egg yolk peptides. Additionally, it has been found that BLP partially hydrolyzed α-la released amphiphilic peptides could self-assemble into micelle structures at a low CMC (0.75 mg/L). , Partial hydrolysis exposes the hydrophobic moieties of α-la, leading to the self-assembly of these peptides into micelles through hydrophobic interactions .…”

“…(e) Self-assembled egg yolk peptide micellar nanoparticles as a versatile emulsifier for the formation and stability of high-internal-phase emulsions. Reproduced with permission from ref . Parts a, b, d: Copyright 2022, 2019, and 2018 Elsevier.…”

“…The compact adsorption of EYPNs could explain the outstanding stability at the interface and the formation of a three-dimensional network. 53 5.3. FPDMPs Enhance the Solubility and Bioactivity of Hydrophobic Nutraceuticals.…”

Novel extraction technologies and potential applications of egg yolk proteins

“…Enzymatic hydrolysis significantly improved the solubility and emulsifying properties of hydrolysates. The authors also used the enzymatic hydrolysis of trypsin to obtain the EHT (Liu et al, 2021 ). The amphiphilic peptides exhibited self-assembly behaviors into micellar nanoparticles with various sizes, depending on the pH values.…”