Toopcham, T., Roytrakul, S. and Yongsawatdigul, J. (2015) Characterization and Identification of Angiotensin I-Converting Enzyme (Ace) Inhibitory Peptides Derived from Tilapia Using Virgibacillus Halodenitrificans sk1-3-7 Proteinases. Journal of Functional Foods, 14, 435-444.
https://doi.org/10.1016/j.jff.2015.01.050

has been cited by the following article:

• TITLE: Purification and Molecular Docking Study of Angiotensin-I Converting Enzyme (ACE) Inhibitory Peptide from Alcalase Hydrolysate of Hazelnut (Corylus heterophylla Fisch) Protein

  AUTHORS: Chunlei Liu, Yan Yu, Fang Liu, Lixin You

  KEYWORDS: Hazelnut Protein, Angiotensin-I-Converting Enzyme Inhibition, Purification, Molecular Docking

  JOURNAL NAME: Food and Nutrition Sciences, Vol.10 No.11, November 29, 2019

  ABSTRACT: Although a number of bioactive peptides are capable of angiotensin I-converting enzyme (ACE) inhibitory effects, little is known regarding the mechanism of hazelnut peptides using molecular simulation. In the present study, gel filtration chromatography, reverse phase-high performance liquid chromatography, and liquid chromatography-electrospray ionization-tandem mass (LC-ESI-MS/MS) were employed for purifying and identifying the ACE inhibitory peptides from hazelnut. To understand the mode of action of these peptides, the interaction between the inhibitory peptides and ACE was investigated. The results identified novel ACE inhibitory peptides Asp-Asp-Glu-Leu-Arg-Gln-Ala (DDELRQA), Asp-Asp-Glu-Leu-Arg-Ala-Ala (DDELRAA), and Asp-Gly-Glu-Leu-Arg-Glu (DGELRE). The binding free energies of DDELRQA, DDELRAA, and DGELRE for ACE were -10.2, -9.0, and -8.8 kcal/mol, respectively. This study proves the high stability of ACE inhibitory peptides derived from hazelnut against different temperature and pH of processing.