| Many bioactive peptides have been reported from various food proteins through the conventional activity-guided-purification approach; however, the rationale behind the selection of conditions for the production of the bioactive peptides has not been extensively explored. The purposes of the study were to provide the rationale behind the selection of conditions, and to develop an innovative strategy to explore the most potent peptides within egg proteins through an integrated QSAR and bioinformatics approach. Thermolysin-pepsin hydrolysate of ovotransferrin was predicted as the best condition for production of ACE-inhibitory peptides. Three predicted peptides, IRW, LKP and IQW, were successfully released from ovotransferrin. Simulated gastrointestinal incubation showed IQW was stable while IRW and LKP can be degraded into dipeptides (IR and KP respectively). Peptides produced from the study will have the potential to be developed as functional foods and nutraceuticals for the prevention of hypertension, a disease affecting ∼31% of the adult population. |
