Micrometer-Sized Fibrillar Protein Aggregates from Soy Glycinin and Soy Protein Isolate

• DOI: 10.1021/jf0718897
• Publication Date: 2007-10-30T03:27:03Z
• Authors: C. Akkermans; A. J. Van der Goot; P. Venema; H. Gruppen; J. M. Vereijken; E. Van der Linden; R. M. Boom
• Keywords: Soy flour

Long, fibrillar semiflexible aggregates were formed from soy glycinin and protein isolate (SPI) when heated at 85 °C pH 2. Transmission electron microscopy analysis showed that the contour length of fibrils was ∼1 µm, persistence 2.3 thickness a few nanometers. Fibrils SPI more branched than glycinin. Binding fluorescent dye Thioflavin T to β-sheets present in fibrils. The presence resulted an increase viscosity shear thinning behavior. Flow-induced birefringence measurements behavior under flow can be described by scaling relations derived for rodlike macromolecules. fibril formation could influenced concentration heating time. Most properties are comparable β-lactoglobulin