Purification identification and function analysis of ACE inhibitory peptide from Ulva prolifera protein

In the present study, Ulva prolifera, an edible alga, was used to prepare angiotensin-I converting enzyme (ACE) inhibitory peptide. The algae protein was isolated and later hydrolyzed by five commercial enzymes (alcalase, papain, pepsin, trypsin, neutral protease), either individually or in combination. Hydrolysate, with the highest in vitro ACE inhibitory activity, was processed using the Sephadex-G100, ultrafiltration, HPLC-Q-TOF-MS, ADMET screening and molecular docking, respectively. The ACE inhibitory peptide DIGGL with a IC50 value of 10.32 +/- 0.96 mu M was then identified. The peptide against ACE by a non-competitive mode and mainly attributable to the three Conventional Hydrogen Bonds. It could activate Endothelial nitric oxide synthase activity in NO generation and reduce Endothelin-1 secretion induced by Angiotensin II in Human umbilical vein endothelial cells. Meanwhile, DIGGL could promote mice splenocytes proliferation, which was also effective when co-incubated with Con A or LPS, respectively. Besides, the anti-ACE peptide could remain active during the digestion of gastrointestinal proteases (pepsin-trypsin) in vitro.

Automated summary

In this study, Ulva prolifera, an edible alga, was used to prepare angiotensin-I converting enzyme (ACE) inhibitory peptide. The highest ACE inhibitory activity was obtained from the hydrolysate of algae protein, which was processed using various methods and identified as the peptide DIGGL. DIGGL exhibited non-competitive inhibition against ACE and mainly achieved this effect through three conventional hydrogen bonds. It also showed the ability to activate endothelial nitric oxide synthase and decrease endothelin-1 secretion in human umbilical vein endothelial cells. Moreover, DIGGL promoted splenocyte proliferation and remained active during gastrointestinal protease digestion.