Effects of high acyl gellan gum on the rheological properties, stability, and salt ion stress of sodium caseinate emulsion.

Sodium caseinate (SC) is widely used as a biological macromolecular emulsifier in oil-in-water (O/W) emulsions. However, the SC-stabilized emulsions were unstable. High-acyl gellan gum (HA) is an anionic macromolecular polysaccharide that improves emulsion stability. This study aimed to investigate the effects of HA addition on the stability and rheological properties of SC-stabilized emulsions. Study results revealed that HA concentrations >0.1 % could increase Turbiscan stability, reduce the volume average particle size, and increase the zeta-potential absolute value of the SC-stabilized emulsions. In addition, HA increased the triple-phase contact angle of SC, transformed SC-stabilized emulsions into non-Newtonian fluids, and effectively inhibited the movement of emulsion droplets. The effect of 0.125 % HA concentration was the most effective, allowing SC-stabilized emulsions to maintain good kinetic stability over a 30-d period. NaCl destabilized SC-stabilized emulsions but had no significant effect on HA-SC emulsions. In summary, HA concentration had a significant effect on the stability of SC-stabilized emulsions. HA altered the rheological properties and reduced creaming and coalescence by forming a three-dimensional network structure, increasing the electrostatic repulsion of the emulsion and the adsorption capacity of SC at the oil-water interface, and thereby improving the stability of SC-stabilized emulsions during storage and in the presence of NaCl.

Effect of Hydrothermal Treatment on the Structure and Functional Properties of Quinoa Protein Isolate.

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.

Ultrasonic Assisted Extraction of Quinoa (Chenopodium quinoa Willd.) Protein and Effect of Heat Treatment on Its In Vitro Digestion Characteristics.

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.