Fuente: PubMed "meat" Food Chem. 2026 Mar 24;513:149016. doi: 10.1016/j.foodchem.2026.149016. Online ahead of print.ABSTRACTThe abundance of water- and salt-insoluble proteins in animal derived by-products limits their high-value utilization. This study aimed to enhance the solubility of chicken liver insoluble proteins (CLIPs) by altering their structure using pH-shifting modification. The results showed that pH shifting affected the physicochemical properties of CLIPs. Notably, compared to the control, alkaline treatment significantly enhanced protein solubility and absolute zeta potential while concurrently decreasing particle size, turbidity and protein aggregation compared to the control (P < 0.05). Structural changes indicated that alkaline treatment induced an unfolding of CLIPs, evidenced by a decreased α-helix content, a concomitant rise in β-sheet and random-coil fractions, and greater exposure of aromatic residues and hydrophobic patches. Furthermore, the exposure of hydrophilic amino acids enhanced hydration capacity, thereby improving protein solubility. Accordingly, this work offers an effective strategy for the solubilization of CLIP through controlled structural unfolding, paving the way for its broader utilization in food-processing applications.PMID:41905233 | DOI:10.1016/j.foodchem.2026.149016