Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 55, Issue 24, Pages 9877-9882Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf0718897
Keywords
soy glycinin; soy protein isolate; aggregation; fibrils; birefringence; TEM; Thioflavin T; viscosity
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Long, fibrillar semiflexible aggregates were formed from soy glycinin and soy protein isolate (SPI) when heated at 85 degrees C and pH 2. Transmission electron microscopy analysis showed that the contour length of the fibrils was similar to 1 mu m, the persistence length 2.3 mu m, and the thickness a few nanometers. Fibrils formed from SPI were more branched than the fibrils of soy glycinin. Binding of the fluorescent dye Thioflavin T to the fibrils showed that beta-sheets were present in the fibrils. The presence of the fibrils resulted in an increase in viscosity and shear thinning behavior. Flow-induced birefringence measurements showed that the behavior of the fibrils under flow can be described by scaling relations derived for rodlike macromolecules. The fibril formation could be influenced by the protein concentration and heating time. Most properties of soy glycinin fibrils are comparable to beta-lactoglobulin fibrils.
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