Isolation and characterization of a new potential source of bioactive peptides: White mulberry (Morus alba) fruits and its leaves

•White mulberry and leaf proteins appear to be a rich source of bioactive peptides.•Presence of bioactive compounds suggest its use as functional ingredient.•White mulberry and leaf proteins shows ACE-inhibition and antioxidant activities.•Extraction efficiency of white mulberry affects the ACE-inhibitory peptides. In this study, white mulberry (WM; Morus alba L.) and its leaf (WML) were hydrolyzed using enzymes at different preheating temperatures (50, 60, 70, 80, and 90 °C) with distilled water at a ratio of 1:10 (w/v). Pepsin, trypsin, chymotrypsin, and alcalase were employed for enzymatic hydrolysis, aiming to investigate the impact of heat treatment and enzymatic hydrolysis on bioactive properties; in particular, angiotensin-converting enzyme-inhibitory (ACE-i) and antioxidant activities. The highest hydrolysis efficiency was observed when using pepsin. The smaller peptides with