%0 Journal Article
%T Collaborative optimization and molecular docking exploration of novel ACE-inhibitory peptides from bovine milk by complex proteases hydrolysis
%A Chunju Bao
%A Guowei Shu
%A He Chen
%A Li Chen
%A Wenfei Shangguan
%J Artificial Cells, Nanomedicine, and Biotechnology
%D 2020
%R https://doi.org/10.1080/21691401.2019.1699824
%X Abstract Food-originated angiotensin-I-converting enzyme (ACE)-inhibitory peptides to preserve hypertension are widely investigated over the past decade. Our research aims to discovery novel ACE-inhibitory peptides from bovine milk by couple of complex proteases (alcalase and protease). By means of response surface methodology with the conditions of pH 9.01, 61.81£¿¡ãC and 6.5% ratio of enzyme to substrate, the hydrolysis model contributes to best-performing ACE-inhibitory activity of 85.02%. Through the further purification by consequent ultrafiltration, macroporous resin and gel chromatography, fraction G2-2 is eventually obtained with ACE-inhibitory activity as high as 92.7%. Two novel peptides of VLPVPQ and VAPFPE are identified by Q-Exactive LC¨CMS/MS. The molecular docking study further suggests that two novel peptides have good combinations of the S1 and S2 active site pockets and Zn(II) of ACE. Our study provides a fitted mathematical model to produce two novel milk-derived ACE-inhibitory peptides, potentially developing the functional foods, especially for hypertension therapy as initial treatment
%U https://www.tandfonline.com/doi/full/10.1080/21691401.2019.1699824