protein isolate

ace inhibitory

functional properties

Food Research International

Protein susceptibility to in vitro gastrointestinal digestion of ovomucin-depleted egg white (OdEW) adjusted to pH 4, 5, 7 and 9 and processed by heat (60 and 80 °C for 10 min) or pulsed electric fields (PEF) (1.4–1.8 kV/cm, 259–695 kJ/kg) was studied by assessing peptide production, proteolytic pattern, and the final peptide profile. Ovotransferrin was more susceptible to pepsin hydrolysis than lysozyme, with ovalbumin showing the highest proteolytic resistance. Ovalbumin was, however, hydrolyzed by pancreatin to produce a stable fragment. Heat treatment of OdEW solutions at 60 °C had little impact on protein susceptibility with the ovalbumin dimers formed having a comparable resistance to pepsinolysis as ovalbumin. Heating at 80 °C significantly enhanced protein susceptibility, as ovalbumin and protein aggregates formed were completely hydrolyzed within 30 min of pepsinolysis. Adjusting OdEW solution to pH 4 and treating with PEF at 695 kJ/kg enhanced protein susceptibility, similar to heat treatment at 80 °C, mainly owing to the enhanced enzymatic hydrolysis of ovalbumin. PEF processing can, therefore, increase protein digestion while minimizing protein aggregation, which will enhance protein functionality in egg whites.

Proteolytic pattern, protein breakdown and peptide production of ovomucin-depleted egg white processed with heat or pulsed electric fields at different pH