Hesperidin (HES) is a citrus flavanone glycoside with promising bioactivities but limited aqueous solubility, which restricts its utilization in food systems. Here, a solvent-free pH-driven strategy was developed to encapsulate HES using ovalbumin (OVA) as a protein carrier, and the structural responses and antioxidant performance of the resulting OVA-HES systems were systematically evaluated at the alkaline driving stage (pH 12) and after neutralization (pH 7). Encapsulation efficiency (EE) increased monotonically at pH 12 and reached 74.75% at 0.8 mg/mL HES, whereas EE exhibited a bell-shaped dependence after neutralization and peaked at 51.64% at 0.6 mg/mL. Fluorescence quenching, Stern-Volmer analysis and docking collectively supported complex formation dominated by static quenching and multiple hydrogen-bond interactions, with stronger binding at pH 12 (K = 49.3 × 10¹⁰ L/mol) than at pH 7 (K = 3.45 × 10¹⁰ L/mol). Moderate HES loading enhanced free sulfhydryl exposure (maximum at 0.6 mg/mL) and improved 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) cation radical scavenging ability, with a peak value of 64.51% at pH 7. Fourier transform infrared spectroscopy, water-holding capacity, low-field nuclear magnetic resonance, and scanning electron microscope analyse further indicated that intermediate HES levels (0.4–0.6 mg/mL) promoted a denser and more continuous gel network, whereas excessive HES induced heterogeneous aggregation and reduced water retention. Overall, this work demonstrates a pH- and dosage-dependent route for incorporating HES into OVA matrices and provides mechanistic insights for designing antioxidant protein gels via solvent-free encapsulation.

Antifreeze peptides (AFP) constitute a unique category of small-molecule proteins or protein hydrolysates that shield organisms from harm induced by freezing or sub-freezing conditions. The heightened effectiveness of AFP compared to traditional commercial antifreeze agents and natural antifreeze proteins has sparked a surge in research interest in recent years. This burgeoning enthusiasm has driven significant advancements in AFP research, paving the way for their potential industrial utilization within the food sector. This review provides a comprehensive exploration of the source of AFP, assesses their antifreeze capabilities, elucidates their mechanisms of action, outlines various preparation methods, and scrutinizes their diverse applications in the food industry. Furthermore, it delves into the prospects for the development and application of AFP, shedding light on the trajectory for ongoing and future research endeavors.

Soybean protein film has good mechanical properties and is an environment-friendly edible packaging material. However, its antibacterial and antioxidant properties are poor, which limits its application to perishable food packaging. In this study, composite films were prepared from soy protein isolate (SPI) as the film-forming substrate with different amounts of an enzymatic hydrolysate of eggshell membrane (ESM) added, and their physical and functional properties were investigated such as mechanical, barrier and optical properties, contact angle, free radical scavenging capacity and antibacterial zone diameter. Fourier transform infrared (FTIR) spectroscopy, X-ray diffraction (XRD) and scanning electron microscopy (SEM) were used to characterize their structures. Finally, we discussed the effect and mechanism of ESM hydrolysate concentration on the structure and properties of composite films. The results showed that the thickness, tensile strength, elongation at break and contact angle of the composite film with 4 g/100 g enzymatic hydrolysate increased by 115.38%, 100.78%, 57.87% and 110.42% respectively compared with pure SPI film, and the water vapor permeability (WVP) and oxygen permeability (OP) decreased by 63.54% and 84.07%, respectively. The antioxidant and antibacterial properties of composite films increased with increasing hydrolysate concentration, and the surface exhibited a dense network structure, due to the formation of intermolecular hydrogen bonds, and good compatibility between SPI and ESM hydrolysate. The results of this study will provide a theoretical basis and technical support for designing active packaging for perishable foods and comprehensive utilization of egg by-products.

As a high nutritional value egg processing product, egg yolk powder has a wide range of applications, However, its emulsification is affected by the processing conditions and is not satisfactory, which limits its wide application in the food industry. Based on this, this paper presents a systematic review of emulsification modification techniques for egg yolk powder, including physical, chemical, and enzyme modification techniques, to improve its emulsification properties and processing adaptability, and to provide a reference for solving such problems. The characteristics of various modification methods were analysed and compared. Future research should focus on optimising the modification process, gaining a deeper understanding of the modification mechanism and developing more mechanisms for the joint application of modification techniques, to maximise the application potential of egg yolk powder and to meet the growing and diversified needs of the food industry.