Use of high pressure to enhance the proteolysis and release of bioactive peptides from ovalbumin and effect of gastrointestinal digestion on the antihypertensive properties of the peptides

摘要: Summary Enzymatic hydrolysis of food proteins can release peptides able to exert different biological activities. Among the bioactive known so far, those with angiotensin converting enzyme (ACE)inhibitory properties are receiving special attention due their potential beneficial effects in treatment hypertension. In previous work we identified active peptide sequences that derive from ovalbumin by enzymatic hydrolysis. We have now explored possibility using high hydrostatic pressure change proteolytic pattern and promote peptides. Pressurization up 400 MPa during treatments greatly enhanced its resulting exerted a considerable ACE inhibition vitro. Hydrolysis under changed led transient accumulation intermediate hydrophobic products. addition, also evaluated impact gastrointesti nal digestion on integrity activity two derived ovalbumin, YAEERYPIL RADHPFL, inhibit vitro exhibit vivo antihypertensive spontaneously hypertensive rats (SHR). Our aim was further understand elucidate whether intact had physiological relevance blood regulation. The results showed both were susceptible degradation after incubation pepsin pancreatic extract. Furthermore, ACEinhibitory decreased simulated digestion. SHR end products gastrointestinal YPI RADHP, respectively, evaluated. Both significantly pressure, 2 hours administration, at doses mg/kg, but probably they did not effect through an ACE-inhibitory mechanism.