Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 60, Issue 20, Pages 5229-5236Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf300367k
Keywords
whey protein self-assembly; amyloid-like fibrils; seeding calcium; ionic strength; rheology; transmission electron microscopy
Funding
- Fonterra Cooperative Ltd.
- New Zealand Foundation for Research, Science and Technology [DRIX0701]
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Amyloid-like fibrils from beta-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 CaCl2. 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.
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