FOOD SCIENCE ›› 2020, Vol. 41 ›› Issue (12): 129-135.doi: 10.7506/spkx1002-6630-20190507-050

• Bioengineering • Previous Articles     Next Articles

Identification and Mechanism of Action of Angiotensin-? Converting Enzyme Inhibitory Peptides from Hen Egg Proteins

YU Zhipeng, FAN Yue, ZHAO Wenzhu, ZHANG Xinyue, LIU Jingbo   

  1. (1. National & Local Joint Engineering Research Center of Storage, Processing and Safety Control Technology for Fresh Agricultural and Aquatic Products, College of Food Science and Engineering, Bohai University, Jinzhou 121013, China; 2. Lab of Nutrition and Functional Food, Jilin University, Changchun 130062, China)
  • Online:2020-06-25 Published:2020-06-22

Abstract: In this study, in silico methods were used to discover novel angiotensin-? converting enzyme (ACE) inhibitory peptides from hen eggs for regulation of blood pressure. Hen egg proteins were in silico hydrolyzed using ExPASy PeptideCutter program. Potential activity, solubility, and absorption, distribution, metabolism, excretion, and toxicity (ADMET) properties of the generated peptides were predicted using program online. Three novel ACE inhibitory peptides, FQK, WGK and ADW, were identified from hen egg protein with IC50 values of (250 ± 0.25), (222.74 ± 1.02) and (85.38 ± 0.54) μmol/L, respectively. The molecular docking studies revealed that the ACE inhibitory activity of FQK, WGK and ADW was mainly attributed to their ability to form very strong hydrogen bonds with the S1 an S2 pockets. This study provides a high-throughput screening method for the identification of food-derived ACE inhibitory peptides.

Key words: hen egg proteins, virtual screening, angiotensin-? converting enzyme inhibitory peptides, pocket site, molecular docking

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