No abstract

The camellia seed cake proteins (CP) used in this study were individually hydrolyzed with neutral protease, alkaline protease, papain, and trypsin. The results showed that the hydrolysate had the highest ACE inhibitory activity at 67.36 ± 0.80% after four hours of neutral protease hydrolysis. Val-Val-Val-Pro-Gln-Asn (VVVPQN) was then obtained through ultrafiltration, Sephadex G-25 gel chromatography separation, LC-MS/MS analysis, and in silico screening. VVVPQN had ACE inhibitory activity with an IC50 value of 0.13 mg/mL (198.66 μmol/L), and it inhibited ACE in a non-competitive manner. The molecular docking indicated that VVVPQN can combine with ACE to form eight hydrogen bonds. The results of the stability study showed that VVVPQN maintained high ACE-inhibitory activity in weakly acidic and neutral environments and that heat treatment (20–80 °C) and Na+, Mg2+, as well as Fe3+ metal ions had little effect on the activity of VVVPQN. Moreover, it remained relatively stable after in vitro simulated gastrointestinal digestion. These results revealed that VVVPQN identified in camellia seed cake has the potential to be applied in functional food or antihypertensive drugs.