The aim of this study was to investigate the effects of hydrothermal treatment at different temperatures and times on the structure and functional properties of quinoa protein isolate (QPI). The structure of QPI was investigated by analyzing changes in the intrinsic fluorescence spectrum, ultra-violet (UV) spectrum, and Fourier transform infrared spectrum. The solubility, water/oil-holding capacity, emulsifying activity, and emulsion stability of QPI were studied, as were the particle size and the thermogravimetric properties of QPI. The results showed that the average particle size of QPI gradually increased with the increase in hydrothermal treatment time and temperature, and reached a maximum value of 121 °C for 30 min. The surface morphology also became rough and its thermal stability also increased. The endogenous fluorescence and UV spectral intensity at 280 nm decreased gradually with increasing hydrothermal treatment time and temperature, and reduced to the minimum values at 121 °C for 30 min, respectively. After hydrothermal treatment, the secondary structure of QPI tended to be disordered. The functional properties of QPI after treatment were all superior to those of the control. The results of this study might provide a basis for the processing and utilization of QPI.

To extract and utilise the protein in quinoa efficiently, we investigated the effect of rate of quinoa protein isolate (QPI) extraction by ultrasound-assisted alkaline extraction and traditional alkaline extraction methods using single-factor experiments and Box-Behnken design. The effect of different heat treatment temperature and time on QPI functional properties and in vitro digestion characteristics were also investigated. The results showed that the optimal conditions of ultrasound- assisted alkaline extraction process were: ultrasonic time 99 min, solid-liquid ratio 1:20 w:v, ultrasonic temperature 47 °C, and pH 10, and its extraction rate and purity were 74.67 ± 1.08% and 87.17 ± 0.58%, respectively. It was 10.18% and 5.49% higher than that of the alkali-soluble acid precipitation method, respectively. The isoelectric point (pI) of QPI obtained by this method was 4.5. The flexibility and turbidity of QPI had maximum values at 90 °C, 30 min, and 121 °C, 30 min, which were 0.42 and 0.94, respectively. In addition, heat treatment changed the 1.77–2.79 ppm protein characteristic region in QPI’s nuclear magnetic resonance hydrogen spectroscopy (¹H NMR). After heating at 90 °C and 121 °C for 30 min, the hydrolysis degree and total amino acid content at the end of digestion (121 °C, 30 min) were significantly lower than those of untreated QPI by 20.64% and 27.85%. Our study provides basic data for the efficient extraction and utilisation of QPI.

The edible film (LBL film) was prepared by layer-by-layer self-assembly technology using Sodium alginate (SA) and ε-polylysine (ε-PL) as polyanion and polycation, respectively. The self-assembly method was optimized, the mechanical and physical properties of the optimal LBL film were characterized, and its preservation effect on blueberry was explored. Results suggested that the transmittance of LBL2 film was above 85%, and the appearance was smooth and transparency consistent. We found that the structure was compact and uniform through scanning electron microscopy (SEM). Differential scanning calorimetry (DSC) showed that LBL2 film had excellent thermal stability. And had lower water solubility and inhibitory effect on Alternaria. LBL2 films were significantly effective at inhibiting the growth of mold and maintain the firmness of postharvest blueberries. Compared with the control group, LBL2 films could prolong the shelf life of a blueberry by 1~2 days at room temperature.

Sodium caseinate (SC)-stabilized emulsions are highly susceptible to flocculation and phase separation near the protein isoelectric point (pI), limiting their application in acidified food systems. In this study, high acyl gellan gum (HA) was introduced to construct pH-responsive protein–polysaccharide complexes to modulate the interfacial assembly and stability of SC emulsions. Results demonstrated that HA interacts with SC primarily through electrostatic attraction and multi-site hydrogen bonding. This interaction induces protein conformational rearrangement and, as evidenced by combined structural and computational analyses, facilitates the assembly of a denser, interconnected composite network. The formation of HA–SC complexes significantly enhanced interfacial adsorption, reduced oil–water interfacial tension. Rheological and microrheological analyses revealed the composite system formed an elasticity-dominated weak gel network, restricting droplet mobility and suppressing aggregation. Consequently, HA–SC emulsions exhibited markedly improved pH tolerance and physical stability compared to SC-only emulsions, particularly near the pI, evidenced by reduced droplet size, lower Turbiscan stability indices, and more homogeneous microstructures. Crucially, utilizing a well-defined mechanistic model of fixed HA and SC concentrations, this study quantitatively links molecular interactions, interfacial network reconstruction, and macroscopic emulsion stability across a broad pH continuum. Rank-correlation analysis of pH-resolved descriptors shows the molecular charge state co-varies monotonically with the interfacial network and macroscopic stability, and is inversely coupled to droplet mobility. These findings provide new insights into protein–polysaccharide interfacial engineering, establishing the essential physical-stability foundation for the future rational design of acid-tolerant food emulsions and functional delivery systems.