Shear-Driven Multiscale Customization of Protein Fibrils: Constructing Bicontinuous Aerogels
摘要
This study investigates the structural regulation of whey protein fibrils (WPF) via shear modification, revealing how shear forces govern their hierarchical organization from molecular to macroscopic scales. Mechanistically, shear treatment induces a critical rheological transition in the fibril network from an elastic gel (tanδ < 1) to a viscoelastic fluid state (tanδ > 1), accompanied by a reduction in aggregate size to ~ 273 nm at 20,000 rpm. At the molecular level, X-ray diffraction reveals shear treatment exerted negligible influence on the cross-β structure. At the mesoscale, controlling the mixing speed (5000–10,000 rpm) enables the precise tuning of porosity within the bicontinuous emulsion templates; lower rates (5000 rpm) yield uniform, fine pores, while higher rates (10,000 rpm) expand pore size while preserving network connectivity. This hierarchical customization strategy successfully translates into macroscopic aerogels with multiscale porosity. Notably, the optimized WPF-5 aerogels—characterized by dense microporous networks—exhibit a remarkable 4512% increase in soybean oil absorption compared to untreated controls. By integrating microscopic, mesoscopic, and molecular insights, this work provides a robust framework for the precision engineering of multiscale protein-based materials.