Amyloid Form of Ovalbumin Evokes Native Antigen-specific Immune Response in the Host

Conditions Governing Food Protein Amyloid Fibril Formation—Part I: Egg and Cereal Proteins

“…The presence of 20 mM trifluoroacetic acid or 30 mM trichloroacetic acid at room temperature even induces OVA aggregation as evidenced by increased ThT fluorescence and β‐sheet contents (Naeem et al., ). OVA aggregates with increased ThT fluorescence are also formed at room temperature when OVA solutions (pH 2.5) are subjected to continuous shaking for multiple days (Tufail et al., ).…”

“…Incubation of OVA (pH 2.5, room temperature) under continuous shaking for 10 days results in fibrillar structures, whereas aggregates with a suprafibrillar structure are observed after 15 days (Tufail et al., ).…”

“…Heating OVA at 40 to 90 °C and neutral pH decreases the percentage of helical structures, and increases ThT fluorescence (Azakami, Mukai, & Kato, ; Pearce, Mackintosh, & Gerrard, ). Also, incubation of OVA at room temperature (pH 7.0) under continuous shaking for up to 15 days yields aggregates with lower percentages of helical structures and higher levels of ThT fluorescence than the starting material (Tufail et al., ).…”

“…(), the structure of OVA aggregates formed during heating at 75 to 80 °C for 24 hr at neutral pH is compatible with that of semiflexible strings of monomers. Fibrillar aggregates have also been reported to result from incubation (pH 7.0) at room temperature during agitation for 15 days (Tufail et al., ). At low ionic strength, heat‐induced aggregates are weakly branched and with increasing ionic strength, the degree of branching and the flexibility increases (Pouzot et al., ).…”

“…However, Tufail et al. () found aggregation of OVA fibrils over several days to be reversible. After fibril formation (room temperature, pH 2.5 or 7.0) and suspension of the fibrils at pH 7.4, monomeric OVA was released from the fibrils in a slow and steady manner.…”