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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.

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.

Highlights • Foaming and emulsifying properties are linear correlated with glycation degree. • Ultrasound treatment enhanced glycation degree and surface properties of conjugates. • Ultrasound promoted the conversion of α-helices to β-sheets and unfolded structures. • Ultrasound induced the formation of amyloid-like fibrils of conjugates., This study aims to optimize the ultrasound treatment conditions for enhancing the degree of glycation (DG) of ovalbumin (OVA)-xylose conjugates through Maillard reaction and investigate the correlation between DG and functional properties affected by structural changes. The structural and functional properties of classical heating OVA, glycated OVA, ultrasonic treated OVA, and ultrasound-assisted glycated OVA were investigated to explore the interaction mechanism of ultrasound treatment on foaming and emulsifying properties improvement. Results indicated that the ultrasound assistance increased free sulfhydryl content, surface hydrophobicity and particle size of OVA-xylose conjugates, and thus enhancing the surface properties, which were strongly linear correlated with DG under different glycation parameters (pH, xylose/OVA ratio, heating time). Additionally, circular dichroism spectroscopy analysis revealed that ultrasound promoted the conversion of α-helices to β-sheets and unfolded structures, which was consistent with the formation of short amyloid-like aggregates that observed by atomic force microscopy phenomenon. Overall, our study provides new insights into the effects of ultrasound treatment on Maillard-induced protein functional properties enhancement, which may be a new strategy to tune the DG and functionality of protein-saccharide grafts during ultrasound processing.

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.

This study aims to evaluate monovalent (Na+) and divalent (Mg2+) ions regulated ovalbumin (OVA) foaming properties enhancement via the change of protein structural and interfacial properties. The macro and microscopic photographs of samples after homogenization 0 min and 30 min were recorded. Results showed that foaming capacity (FC) significantly increased from 59.44 ± 16.69% to 136.67 ± 11.55% (NaCl) and 117.22 ± 5.36% (MgCl2). Accordingly, viscosity and surface intension reduced, whereas the amount of OVA adsorption increased, which suggested that ions could promote adsorption of OVA to air-water interface and further improve the foaming properties. Analogously, surface hydrophobicity (H0) increased, which revealed that the improvement of hydrophobic interactions of OVA. Besides, the β-sheet content increased, which indicated larger aggregates formed. Noteworthy, from the results of the interfacial adsorption amount and microscopic photographs, the foaming stability (FS) of samples with divalent ions was better, which could be hypothesized that protein intermolecular interactions via salt bridge may be stronger, while monovalent ions interacted with protein by nonspecific bond. Overall, our study provides a convenient approach of ions regulated structural and foaming properties of OVA, which may be a new strategy in improving the protein interfacial properties in food processing industry.