Drying mode and hydrothermal treatment conditions govern the formation of amyloid-like protein fibrils in solutions of dried hen egg white

The recipe of some food products contains dried hen egg white (EW). It is convenient in use and available with a range functionalities as result being stored under different time, temperature moisture conditions following drying. Amyloid fibrils are fibrillary protein structures composed highly ordered stacking cross-? sheets. They can contribute to the foaming gelling capacity EW proteins. We here for first time report that amyloid-like such spray-dried (EWSD) longer (ca. 100–200 nm) than those freeze-dried [EWFD] 20–100 nm). In addition, optimal fibrillation were determined both EWFD ovalbumin (OVAFD) using response surface design. Dilute solutions OVAFD incubated at pH values, times temperatures. After storage [2.0% (wprotein/v), 7.0, 23 h, 76 °C] [0.5% 24 85 °C], higher level sheet larger worm-like observed EWFD. Lastly, when EWSD one week either 50 °C 50% relative humidity (RH) [EWSD 50°C/50%] or 60 80% RH (EWSD 60°C/80%) was submitted heating extent found 60°C/80% 50°C/50%. Thus, drying induces fibrillation. Also dry further enhances during excess water.