• Ultrasound-assisted pH-shifting treatments could reduce particle size and zeta potential of milk protein. • A new modification method improved the solubility of dairy ingredients containing large amounts of casein. • Proteins subjected to ultrasonic treatment at pH 11 had the best surface hydrophobicity. • Combined treatments effectively improved the foaming capacity of milk proteins.

This work investigated the effects of thermal processing methods commonly used in the dairy industry and prolonged treatment at different temperatures on the denaturation, microstructure, and functional properties of whey proteins (WP) from goat milk. The complete denaturation of WP was observed in goat milk treated at 85°C for 30 min, and at a higher temperature (>85°C), a considerable amount of WP was easily denatured. The low temperature, long time treatment had the least effect on the secondary structure, whereas ultra-high temperature treatment had the greatest effect, and the amount of regular structures decreased gradually with prolonged time. The most serious morphological damage occurred after treatment at 85°C for 30 min, which was consistent with the denaturation results. This result indicated that the denaturation degree, particle size, surface hydrophobicity, and microstructure had a strong influence on the functional properties of WP from goat milk after heat treatment. The heat treatment of goat milk at 65°C for 30 min and 85°C for 15 s increased the particle size, turbidity, zeta potential, and surface hydrophobicity of WP, and these increases ensured that the WP had a good emulsifying activity index, water-holding capacity, oil-holding capacity, foaming capacity, and foam stability. This study simulated the heat treatment conditions used in actual production, aiming to provide a theoretical basis for industry.

Graphene oxide (GO) has good dispersibility and adsorption capacity for antibiotics adsorption, a complex process influenced by many factors. In this work, the adsorption mechanism of GO on tetracycline antibiotics at different pH was studied to address its attenuated effects on the microbial growth. The results showed that the adsorption process of GO on three antibiotics, namely, tetracycline (TC), oxytetracycline (OTC), and chlortetracycline (CTC), followed the pseudo-second-order kinetic model. The maximum adsorption capacities were observed at pH5 which were 133.0 mg/g for TC, 125.4 mg/g for OTC, and 167.0 mg/g for CTC. Furthermore, the reaction was uniform adsorption with a single layer on the surface of GO, and heating was conducive to the reaction. In the microbial growth experiment, the growth of E. coli and B. subtilis senses was optimal at pH5, which was consistent with the adsorption experiment. This study analyzed the effect of pH on the adsorption of antibiotics by GO and provided a theoretical basis for the further application of GO in various aquatic environments.

This study was carried out to investigate the effects of pH and heat on the structure and function of milk proteins by comparing goat milk treated under different pH and temperature conditions. The results showed that pH had a significant effect on the thermal stability of goat milk proteins, and the proteins were least thermally stable at pH 7.7. Except for the pH 6.9 goat milk, the surface hydrophobicities of the milk proteins at various pH values reached their maxima at 85°C. The particle size, zeta potential, and content of regular secondary structure also decreased significantly at 85°C, and the turbidity of milk proteins under alkaline pH conditions was lower than that under acidic conditions. It was concluded that alkaline conditions resulted in better emulsion stability and oil-holding capacity, and acidic conditions offered better foaming ability, foam stability, and water-holding capacity for goat milk protein during heat processing. It can also be seen that 85°C was the key temperature for milk proteins after changing the pH of the milk. This paper provides a theoretical basis for optimizing the processing conditions for goat milk and the applications of goat milk proteins.