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Updated: Feb 19, 2026

Microfluidic Mixers for Studying Protein Folding
Published on: April 10, 2012
Solubility and interfacial behavior of myofibrillar proteins modulated by pH-shifting and microfluidization
Lixian Zhang1, Zhenzhen Ge2, Lihua Zhang2
1College of Food and Bioengineering, Zhengzhou University of Light Industry, Zhengzhou 450002, China.
Abstract:
Low solubility and poor interfacial adsorption capacity have constrained the application of myofibrillar proteins (MP) in meat product processing. This study investigated the effects and underlying mechanisms of pH-shifting and dynamic high-pressure microfluidization (DHPM) treatment on the solubility, microstructure, and interfacial behavior of MP. Compared to acidic (pH 3) shifting, significant electrostatic repulsion was induced by alkaline (pH 12) shifting treatment, resulting in enhanced unfolding of MP and greater exposure of hydrophobic groups. The dynamic unfolding and structural reorganization of MP polypeptide chains were further facilitated by the intense shear forces, turbulent flow, and cavitation effects generated by DHPM. Partial degradation of myosin was induced by DHPM treatment, with a reduction in α-helical content and concurrent increases in β-sheet and random coil structures, indicating more extensive conformational rearrangement of the protein. The solubility and particle size of MP after pH shifting were further enhanced by DHPM, with more significant improvements observed in the pH 3-DHPM group. The pH-DHPM synergistic treatment enhanced the interfacial behavior of MP by accelerating its adsorption, diffusion, and penetration at the oil-water boundary. The strong relationship among solubility, surface hydrophobicity, and particle size was revealed by correlation analysis. The pH-DHPM synergistic strategy represented an effective physicochemical approach for modulating the functional properties of MP, offering both theoretical insights and a technical foundation for expanding the utilization of MP in low-salt food systems and high-performance edible film development.
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