Effects of thermal, non-thermal and emulsification processes on the gastrointestinal digestibility of egg white proteins

Egg white proteins (EWPs) are an excellent source of essential amino acids for human nutrition. Also, egg is commonly used in food processing because its numerous technological functionalities. Processing can influence the EWPs digestibility and thereby acid bioavailability. A better understanding effects on enables improving nutritional value EWP products. This review elucidates impact diverse methods at molecular level (individual molecules), supramolecular (aggregated state), macroscopic (gelled state). Heat, high pressure, ultrasound, pulsed electric fields, adsorption interface unfold native EWPs, causing exposure hydrolysis sites improvement protein level. However, Maillard glycation may restrict access digestive enzymes to reduce their digestibility. The reaction also lower IgE-binding capacity ovalbumin, which could potentially allergenicity. At level, protein-protein interactions between unfolded lead formation aggregates with different morphologies, depending pH ionic strength. accessibility cleavage heat-induced spherical compared linear counterparts. gels formed from show resistance digestion owing dense network these gels. combination processes increase For instance, quick production specific bioactive peptides be achieved by applying enzymatic treatment under pressure.