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Purification and Molecular Docking Study of Angiotensin-I Converting Enzyme (ACE) Inhibitory Peptide from Alcalase Hydrolysate of Hazelnut (<i>Corylus heterophylla</i>Fisch) Protein 被引量:1

Purification and Molecular Docking Study of Angiotensin-I Converting Enzyme (ACE) Inhibitory Peptide from Alcalase Hydrolysate of Hazelnut (<i>Corylus heterophylla</i>Fisch) Protein
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摘要 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. 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.
出处 《Food and Nutrition Sciences》 2019年第11期1374-1387,共14页 食品与营养科学(英文)
关键词 HAZELNUT PROTEIN Angiotensin-I-Converting Enzyme Inhibition PURIFICATION MOLECULAR Docking Hazelnut Protein Angiotensin-I-Converting Enzyme Inhibition Purification Molecular Docking
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