4.7 Article

Whey Protein Nanofibrils: The Environment-Morphology-Functionality Relationship in Lyophilization, Rehydration, and Seeding

Journal

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 60, Issue 20, Pages 5229-5236

Publisher

AMER CHEMICAL SOC
DOI: 10.1021/jf300367k

Keywords

whey protein self-assembly; amyloid-like fibrils; seeding calcium; ionic strength; rheology; transmission electron microscopy

Funding

  1. Fonterra Cooperative Ltd.
  2. New Zealand Foundation for Research, Science and Technology [DRIX0701]

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.7
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available