The use of high hydrostatic pressure to promote the proteolysis and release of bioactive peptides from ovalbumin

Enzymatic hydrolysis of food proteins can release peptides able to exert different biological activities. Among the bioactive peptides known so far, those with angiotensin converting enzyme (ACE)-inhibitory properties are receiving special attention due to their potential beneficial effects in the treatment of hypertension. In a previous work, we identified active peptide sequences that derived from proteolysis of ovalbumin. We have now explored the possibility of using high hydrostatic pressure to promote the release of bioactive peptides. Treatment of ovalbumin under high pressures, up to 400 MPa, with chymotrypsin, trypsin and pepsin, enhanced its hydrolysis and changed the proteolytic pattern. However, under the conditions assayed, the in vitro ACE inhibitory activity of the hydrolysates did not improve as compared with those obtained at atmospheric pressure. Nevertheless, proteolysis under pressures of 200–400 MPa accelerated the release of the peptides YAEERYPIL, FRADHPFL and RADHPFL, with demonstrated antihypertensive effects in vivo.