The development of low-viscosity, high-concentration protein systems is hindered by shear-thickening behavior arising from intermolecular entanglement. We report a cyclical preheating-ultrasonication strategy that reconstitutes cod protein (CPs) into low-adhesion particles. Pre-heating (100 °C, 10 min) partially unfolds CPs to expose hydrophobic nucleation sites, followed by ultrasonication (400 W, 10 min) fragmenting aggregates into metastable subunits via cavitation shear while redistributing surface charges. Force curve analysis validated the adhesion force reduction (62.6%, 3.96 → 1.48 nN) and its direct correlation with significant viscosity reduction at high concentration. The modified CPs exhibit Newtonian fluid behavior at 6% w/v concentration, with the viscosity was reduced to approximately 0.1 Pa·s at a scanning frequency of nearly 1 s-1. Small-angle X-ray scattering (SAXS) shows a structural shift from loose aggregates to dense molten spheres. This physical reprocessing approach provides a sustainable pathway to engineer high-density protein colloids for injectable formulations and 3D food printing.
Abstract
Journal Article
eng
42102458
Yu, Xueer, et al. "Aggregation-disaggregation Cycling: a Physical Strategy for Low-viscosity Fish Protein Particles." Food Chemistry, vol. 517, 2026, p. 149487.
Yu X, Zhao X, Zou B, et al. Aggregation-disaggregation cycling: A physical strategy for low-viscosity fish protein particles. Food Chem. 2026;517:149487.
Yu, X., Zhao, X., Zou, B., Jian, A., Li, J., Xu, X., Du, M., Wu, C., & Na, X. (2026). Aggregation-disaggregation cycling: A physical strategy for low-viscosity fish protein particles. Food Chemistry, 517, 149487. https://doi.org/10.1016/j.foodchem.2026.149487
Yu X, et al. Aggregation-disaggregation Cycling: a Physical Strategy for Low-viscosity Fish Protein Particles. Food Chem. 2026 Jul 15;517:149487. PubMed PMID: 42102458.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR
T1 - Aggregation-disaggregation cycling: A physical strategy for low-viscosity fish protein particles.
AU - Yu,Xueer,
AU - Zhao,Xinyao,
AU - Zou,Bowen,
AU - Jian,Aijun,
AU - Li,Jiaxin,
AU - Xu,Xianbing,
AU - Du,Ming,
AU - Wu,Chao,
AU - Na,Xiaokang,
Y1 - 2026/05/03/
PY - 2025/8/26/received
PY - 2026/2/23/revised
PY - 2026/5/2/accepted
PY - 2026/5/28/medline
PY - 2026/5/9/pubmed
PY - 2026/5/8/entrez
KW - Cod protein
KW - High protein concentration
KW - Low-viscosity
KW - Molten globule state
KW - Preheating and ultrasonic
SP - 149487
EP - 149487
JF - Food chemistry
JO - Food Chem
VL - 517
N2 - The development of low-viscosity, high-concentration protein systems is hindered by shear-thickening behavior arising from intermolecular entanglement. We report a cyclical preheating-ultrasonication strategy that reconstitutes cod protein (CPs) into low-adhesion particles. Pre-heating (100 °C, 10 min) partially unfolds CPs to expose hydrophobic nucleation sites, followed by ultrasonication (400 W, 10 min) fragmenting aggregates into metastable subunits via cavitation shear while redistributing surface charges. Force curve analysis validated the adhesion force reduction (62.6%, 3.96 → 1.48 nN) and its direct correlation with significant viscosity reduction at high concentration. The modified CPs exhibit Newtonian fluid behavior at 6% w/v concentration, with the viscosity was reduced to approximately 0.1 Pa·s at a scanning frequency of nearly 1 s-1. Small-angle X-ray scattering (SAXS) shows a structural shift from loose aggregates to dense molten spheres. This physical reprocessing approach provides a sustainable pathway to engineer high-density protein colloids for injectable formulations and 3D food printing.
SN - 1873-7072
UR - https://www.unboundmedicine.com/prime/citation/42102458/Aggregation-disaggregation_cycling:_A_physical_strategy_for_low-viscosity_fish_protein_particles.
DB - PRIME
DP - Unbound Medicine
ER -


