Whey Protein Nanofibrils: The Environment–Morphology–Functionality Relationship in Lyophilization, Rehydration, and Seeding
Simon M. Loveday, Jiahong Su, M.A. Rao, Skelte G. Anema, Harjinder Singh
Journal of Agricultural and Food Chemistry
Abstract
Amyloid-like fibrils from β-lactoglobulin have potential as efficient thickening and gelling agents for food and biomedical applications, but the link between fibril morphology and bulk viscosity is poorly understood. We examined how lyophilization and rehydration affects the morphology and rheological properties of semiflexible (i.e., straight) and highly flexible (i.e., curly) fibrils, the latter made with 80 mM CaCl(2). Straight fibrils were fractured into short rods by lyophilization and rehydration, whereas curly fibrils sustained little damage. This was reflected in the viscosities of rehydrated fibril dispersions, which were much lower for straight fibrils than for curly fibrils. Lyophilized straight or curly fibrils seeded new fibril growth, but viscosity enhancement due to seeding was negligible. We believe that the increase in fibril concentration caused by seeding was counterbalanced by a decrease in fibril length, reducing the ability of fibrils to form physical entanglement networks.
Extracted Claims
5 claims extracted from this paper into the knowledge graph
lyophilization and rehydration fractures straight fibrils
“Straight fibrils were fractured into short rods by lyophilization and rehydration”
lyophilization and rehydration sustains curly fibrils
“curly fibrils sustained little damage”
seeding causes increase in fibril concentration
“Lyophilized straight or curly fibrils seeded new fibril growth, but viscosity enhancement due to seeding was negligible. We believe that the increase in fibril concentration caused by seeding was coun...”