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

Zhenqiu Xu; Changping Wu; Dongxiao Sun-Waterhouse; Tiantian Zhao; Geoffrey I N Waterhouse; Mouming Zhao; Guowan Su

doi:10.1016/j.foodchem.2020.128855

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

Food Chem. 2021 May 30:345:128855. doi: 10.1016/j.foodchem.2020.128855. Epub 2020 Dec 10.

Authors

Zhenqiu Xu¹, Changping Wu², Dongxiao Sun-Waterhouse³, Tiantian Zhao³, Geoffrey I N Waterhouse³, Mouming Zhao⁴, Guowan Su⁵

Affiliations

¹ School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China; Guangdong Huapeptide Biotechnology Co., Ltd., Zhaoqing 526238, China.
² School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China; Department of Food Science and Engineering, Jinan University, Guangzhou 510632, China.
³ School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China.
⁴ School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China; Department of Food Science and Engineering, Jinan University, Guangzhou 510632, China; Guangdong Huapeptide Biotechnology Co., Ltd., Zhaoqing 526238, China.
⁵ School of Food Science and Engineering, South China University of Technology, Guangzhou 510640, China; Department of Food Science and Engineering, Jinan University, Guangzhou 510632, China. Electronic address: [email protected].

PMID: 33340899
DOI: 10.1016/j.foodchem.2020.128855

Abstract

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 μM). 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.

Keywords: Activated carbon; Angiotensin-I converting enzyme inhibitor; Molecular docking; Simulated gastrointestinal digestion; Soy protein isolate.

MeSH terms

Angiotensin-Converting Enzyme Inhibitors / analysis*
Angiotensin-Converting Enzyme Inhibitors / metabolism
Angiotensin-Converting Enzyme Inhibitors / pharmacology
Animals
Computer Simulation*
Digestion*
Hydrophobic and Hydrophilic Interactions
Molecular Docking Simulation*
Peptides / analysis*
Peptides / metabolism
Peptides / pharmacology
Peptidyl-Dipeptidase A / chemistry
Peptidyl-Dipeptidase A / metabolism*
Protein Conformation
Soybean Proteins / chemistry*

Substances

Angiotensin-Converting Enzyme Inhibitors
Peptides
Soybean Proteins
Peptidyl-Dipeptidase A