Author(s)

Chunlei Liu^1,2, Yan Yu¹, Fang Liu¹, Lixin You^1*

¹College of Life Sciences, Changchun Sci-tech University, Changchun 130600, P. R. China.
²College of Food Science and Engineering, Jilin Agricultural University, Changchun 130118, P.R. China.

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.

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

Liu, C. , Yu, Y. , Liu, F. and You, L. (2019) Purification and Molecular Docking Study of Angiotensin-I Converting Enzyme (ACE) Inhibitory Peptide from Alcalase Hydrolysate of Hazelnut (Corylus heterophylla Fisch) Protein. Food and Nutrition Sciences, 10, 1374-1387. doi: 10.4236/fns.2019.1011098.