In Vitro Stability of ACE-Inhibitory Peptides of Rohu Fish Waste to Heat, pH and Gastrointestinal Enzymes

Angiotensin-I converting enzyme inhibitory (ACEi) peptides were prepared from rohu (Labeo rohita) fish wastes by enzymatic hydrolysis [1.1% alcalase concentration (v/w); 130 min time; 52degree celsius temperature and 0.8:1 solid-liquid ratio]. Ultrasound Assisted Enzymatic Extraction (UAEE) and Microwave Assisted Enzymatic Extraction (MAEE) were performed to enhance degree of hydrolysis (DH), ACEi activity, and peptide yield (PY). The ACEi peptides were examined for stability during thermal processing, varied pH treatments and in vitro gastrointestinal digestion. Peptides were stable at different temperatures (25, 37, 55, 75, and 100degree celsius) except at 121degree celsius which reduced their stability by 7%, 6.9% and 2.2% in UAEE, MAEE and Non-Assisted Enzymatic Extraction (NAEE) peptides, respectively. Similarly, peptides retained ACEi at pH 2 to 8 and subsequent reduction at pH>8. In vitro digestion studies showed stability of all peptides to GI digestion at 0.05% pepsin, 0.05% trypsin, 0.05% chymotrypsin and the combination of 0.025% trypsin and 0.025% chymotrypsin except MAEE peptides showing less stability with pepsin (0.05%). Therefore, it is concluded that these ACEi peptides derived from rohu fish waste, stable to heat, pH and gastrointestinal enzymatic action, can be used as ingredient in functional foods, which undergo thermal processing and digestion.