Search

Fermented egg milk beverage (FEMB) can alleviate the symptoms of intestinal diseases by regulating intestinal flora and supplying nutrition. This study was investigated in the protective effect of fermented egg milk beverage (FEMB) on dextran sulfate sodium (DSS) induced ulcerative colitis (UC) mice. The results showed that FEMB eased the pathological abnormalities and colonic inflammation of UC mice, restructured the intestinal flora composition simultaneously. After FEMB treatment for 14 days, the body weight of the mice rose and disease activity index (DAI) decreased, the length and form of colon in UC mice restored notably, inflammatory cells were decreased or disappeared, globel cells and crypt were enriched and modified. 16S rRNA gene sequencing results demonstrated that FEMB treatment can increase the abundance of beneficial bacteria in the cecum content of mice, including unclassified_f_Lachnospiraceae and Lactobacillus. Besides, probiotics that can increase the content of short-chain fatty acids (SCFAs) may also contribute to inflammation alleviation. An increasing of amino acid, which may beneficial to nutritional supplement, was observed in our experiment. In conclusion, FEMB treatment can alleviate the damage of DSS-induced colitis in Balb/c mice, this study provides theoretical basis of inflammation relief and application of probiotics in fermented egg milk beverages.

The Maillard reaction reduces the gastrointestinal digestibility of ovalbumin (OVA) in vitro. However, the regulatory effects of OVA and its Maillard reaction products (MRPs) on gut microbiota disorders remain unknown. In this study, the influence of OVA and its MRPs on the modulation of gut microbiota in mice with dextran sulfate sodium (DSS)-induced colitis was investigated. The results revealed that OVA and its MRPs intake could alleviate the symptoms of colitis and improve the richness and diversity of the gut microbiota. Moreover, the results revealed that the Maillard reaction would block the release of lysine and essential amino acids in vivo, but they variously regulated the gut microbiota and the levels of short-chain fatty acids (SCFAs) due to their indigestible properties. These findings provide a basic theory for the rational utilization of OVA and its MRPs as nutraceutical food ingredients in regulating the gut microbiota for maintaining intestinal health.

Egg white derived peptides (EWDP) and curcumin are well known for diverse biological activities, but the combinational usage of the two natural nutraceuticals is extremely limited by their low oral bioavailability and distinctly different polarities. Therefore, this study aimed to exploit a facile self-assembled amphiphilic system for oral co-delivery of hydrophilic egg white derived peptides (EWDP) and hydrophobic curcumin. The hydrophobic curcumin was first loaded into the hydrophobic cavity of β-cyclodextrin (β-CD) as a core. Then, the hydrophilic EWDP was absorbed into the region between the core and the N-[(2-hydroxy-3-trimethyl ammonium) propyl] chitosan (HTCC) shell to form the amphiphilic nanoparticles (NPs) via layer-by-layer self-assembly. The resulting NPs showed ideal oral applicability with excellent colloidal properties and encapsulation capacity for EWDP and curcumin at pH 2.0-7.0. X-ray Photoelectron Spectroscopy (XPS), Fourier transform infrared spectroscopy (FTIR), nuclear magnetic resonance (1H NMR), X-ray diffraction (XRD) and differential scanning calorimetry (DSC) results indicated that hydrogen bonding and hydrophobic interaction were the main driving force for the formation of amphiphilic NPs. Upon combination with HTCC, EWDP (both shell material and core nutraceuticals) could facilitate curcumin loading into the deeper β-CD cavity site with admirable solubility improvement. Moreover, EWDP and curcumin after co-delivery exhibited superior bioavailability (especially for bioactivity and cellular absorption) than the simple mixture and conventional curcumin inclusion complex. Overall, these findings are enlightening for the rational peptide based oral co-delivery system formulations for a broader range of hydrophilic and hydrophobic nutraceuticals (initially synergistic or not) in the food and related health-promoting fields.

Egg-white peptides (EWP,1 kDa) have been shown to possess various bioactive properties. However, poor emulsification of EWP limits its application in functional foods. In this study, EWP aggregation induced by proanthocyanidins (PC) contributed to the improvement of emulsion properties. The two-step binding process of PC-EWP-EWP was confirmed by isothermal titration calorimetry, fluorescence spectroscopy, surface hydrophobicity, and Fourier transform infrared spectroscopy. We found that first EWP combines with PC via hydrogen bonding and hydrophobic interactions. Next, more EWPs bind to the EWP in PC-EWP via hydrogen bonding, thereby forming PC-EWP-EWP aggregates. The aggregates (PC to EWP ratio of 1:4) reduced the surface tension (6 %) and improved the contact angle (53 %). The co-adsorption of EWP and aggregates at the O/W interface improved the contact angle, protein adsorption rate, and emulsion stability. This study establishes EWP aggregates induced by PC as an effective emulsifier, thereby expanding the application fields of EWP.

In this paper, the effects of hydroxyl radical-induced oxidation on structural characteristics, molecular interaction, functional properties, especially in gastric digestibility of egg white protein (EWP) were investigated. Altogether, oxidation enhanced EWP foaming stability, accompanied with even and loose arrangement bubbles by high interfacial and rheological properties. Additionally, structure and morphology characterization of hydrolysates as well as digestion kinetics results indicated the oxidized EWP had greater digestion degree and rate to release more free amino acids, along with hydrolysates composed by smaller globules and fibers. Briefly, oxidation might improve EWP functional and gastric digestive properties by providing more flexible conformation and strengthening non-covalent interactions. This work might provide an enlightening insight for enhancing protein functional properties and the nutrition of EWP via prompting amino acids release for the healthy food design.

Fear memory contextualization is critical for selecting adaptive behavior to survive. Contextual fear conditioning (CFC) is a classical model for elucidating related underlying neuronal circuits. The primary visual cortex (V1) is the primary cortical region for contextual visual inputs, but its role in CFC is poorly understood. Here, our experiments demonstrated that bilateral inactivation of V1 in mice impaired CFC retrieval, and both CFC learning and extinction increased the turnover rate of axonal boutons in V1. The frequency of neuronal Ca

This study aimed to establish binary protein system on egg white ovalbumin (OVA) -lysozyme (LYS), and investigated the relationship between co-aggregation and co-gelation. We focused on the formation of OVA-LYS complex, the typical thermo-dynamically favored coacervation process, in terms of gelling properties, microstructure and thermodynamics. Benefited from synergistic effects during co-gelation, the thermally induced gels of OVA-LYS complex formed at extremely low protein concentration (18 mg/mL) and showed higher storage modulus with increasing LYS concentration. Moreover, the rising particle size, reduced zeta potential, unordered secondary structure and strengthened protein chain were observed with the addition of LYS. Remarkably, the divalent ions enhanced thermodynamic stability of OVA-LYS complex, although the growth of aggregates units were prevented by ions at room temperature. ITC and molecular docking analyses revealed the binding affinity stoichiometry and combination phase, which were closely related to the decrease of minimum energy resulted from the formation of hydrogen bond.

The aim of this study is to develop a dual-functional ingredient with antioxidant activity and emulsification. The emulsion stability of ovalbumin (OVA) was improved by procyanidins (PC). The interactions between OVA and PC were investigated using multi-spectroscopy and molecular docking. Furthermore, the effect of the addition of the OVA-PC mixture on emulsion stability was evaluated as well. The fluorescence results showed that the quenching mechanism of PC to OVA's endogenous fluorescence was static quenching, and the binding ratio of OVA and PC was 1:1. Circular dichroism (CD) and Fourier Transform Infrared Spectrometer (FT-IR) showed that the addition of PC promoted the unfolding of OVA, and transformed the secondary structure of OVA from α-helix to β-sheet. The main driving force of OVA and PC was hydrogen bonding, according to molecular docking analysis. Among all the samples, the stability of the emulsion of OVA-PC at a ratio of 1:30 exhibited extremely high stability and the smallest particle size. In comparison with individual OVA emulsions, the OVA-PC emulsions had excellent physical stabilities. Meanwhile, the oxidation degree of protein and oil for the OVA-PC emulsions was lower than that of the native OVA emulsion after 8-day storage. Our work provides important insights for understanding the interaction between OVA and expanding the application of OVA-PC.

This study aims to evaluate the structure of ions-regulated gelation of egg white protein (EWP) via aggregation kinetics model, which was built by monitoring turbidity. Results showed that compared with NaCl and KCl, the addition of Na

Glycation can improve the functional properties of protein. However, in vitro and animal studies have shown that glycation induced lysine blockage and impaired protein digestibility. This study aimed to explore the effects of different glycation degree on the structure and digestive characteristics of ovalbumin. The results showed that glycation decreased the turbidity and hydrophobicity of the protein and changed the protein structure. Moreover, the results of in vitro simulated digestion revealed that glycation reduced the contents of essential amino acids and total amino acids after digestion. Glycation changed the amino acids and peptides release from the protein by resisting the digestion of digestive enzymes, especially trypsin. In conclusion, this work links glycation, protein digestibility, and the release of amino acids and peptides. This emphasizes the importance of the balance between improving properties and ensuring the digestibility of proteins during food processing.

The mechanism between food gelation and its digestibility has attracted increasing attention over the past few decades. This study aimed to evaluate the effect of glycation degree on the gelation and digestibility of egg white gel (EWG) using an in vitro model and a multi-scale characterization of gel structure. Results showed that EWG glycated with increasing d -ribose by covalent bonds exhibited better gelling properties and lower in vitro digestibility according to the appearance of soluble proteins and peptides. Besides, glycation preference for ovotransferrin at lysine might be important for regulating gel structure and proteolysis accessibility via the ratio of fibrous and granular aggregates. Moreover, gel structure was predominant over amino acids modification for digestibility. Binding disorder and steric hindrance could ascribe to the lower digestibility of gels. These findings are enlightening for the formulation and production of food matrix with controlled digestibility through glycation in food and related pharmaceutical fields.