Identification of post-digestion angiotensin-I converting enzyme (ACE) inhibitory peptides from soybean protein Isolate: Their production conditions and in silico molecular docking with ACE

被引：147
作者：
Xu, Zhenqiu [1 ,3 ]
Wu, Changping [1 ,2 ]
Sun-Waterhouse, Dongxiao [1 ]
Zhao, Tiantian [1 ]
Waterhouse, Geoffrey I. N. [1 ]
Zhao, Mouming [1 ,2 ,3 ]
Su, Guowan [1 ,2 ]
机构：
[1] South China Univ Technol, Sch Food Sci & Engn, Guangzhou 510640, Peoples R China
[2] Jinan Univ, Dept Food Sci & Engn, Guangzhou 510632, Peoples R China
[3] Guangdong Huapeptide Biotechnol Co Ltd, Zhaoqing 526238, Peoples R China
来源：
FOOD CHEMISTRY | 2021年 / 345卷
关键词：
Soy protein isolate; Angiotensin-I converting enzyme inhibitor; Activated carbon; Molecular docking; Simulated gastrointestinal digestion; BIOACTIVE PEPTIDES; OPTIMIZATION; ANTIOXIDANT; PURIFICATION; AGGREGATION; BINDING; RENIN; LEU;
D O I：
10.1016/j.foodchem.2020.128855
中图分类号：
O69 [应用化学];
学科分类号：
081704 ;
摘要：
This study attempts to investigate natural angiotensin-I converting enzyme (ACE) inhibitors. Soybean protein isolated (SPI) hydrolysate (SPIH) was prepared by Alcalase from inexpensive SPI, and their ACE inhibitory peptides were obtained via membrane separation, ethanol precipitation and adsorption chromatography enrichment. Activated carbon was more suitable for peptide enrichment than eight macroporous resins. The peptide fraction yielded under optimal conditions (protein-active carbon mass ratio 2:1; adsorption pH 3.0 and time 2 h; desorption time 2 h) exhibited a 10.4 times higher ACE-inhibitory activity than SPIH. Novel peptides IY, YVVF, LVF, WMY, LVLL and FF (hydrophobicity values 10.51-12.87; activity scores 0.2373-0.999) might be the main contributors to SPIH's ACE inhibition. IY had the lowest IC50 (0.53 +/- 0.02 mu M). YVVF had the greatest affinity (-9.8 kcal/mol) for 2OC2 (ACE's C-domain receptor) via H-bonds. IY and WMY could be potent ACE inhibitors, and their ACE-inhibitory activities unaltered and increased after in vitro gastrointestinal digestion.
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页数：8
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