Abstract
In the present study, a novel angiotensin I-converting enzyme inhibitory (ACE inhibitory) peptide, EPNGLLLPQY, derived from walnut seed storage protein, fragment residues 80–89, was identified by ultra-high performance liquid chromatography electrospray ionization quadrupole time of flight mass spectrometry (UPLC-ESI-Q-TOF-MS/MS) from walnut protein hydrolysate. The IC50 value of the peptide was 233.178 μM, which was determined by the high performance liquid chromatography method by measuring the amount of hippuric acid (HA) generated from the ACE decomposition substrate (hippuryl-l-histidyl-l-leucine (HHL) to assess the ACE activity. Enzyme inhibitory kinetics of the peptide against ACE were also conducted, by which the inhibitory mechanism of ACE-inhibitory peptide was confirmed. Moreover, molecular docking was simulated by Discovery Studio 2017 R2 software to provide the potential mechanisms underlying the ACE-inhibitory activity of EPNGLLLPQY.
Highlights
There is a trend that the number of people with cardiovascular disease (CVD) is increasing year by year
In order to identify the peptides in the walnut hydrolysates, ultra-high-performance liquid chromatography (UPLC)-quadrupole time of flight (Q-TOF)-MS/MS combined with MASCOT searching was used to analyze the fragment spectra [24]
Many kinds of peptides were identified from walnut seed storage protein (Q2TPW5)
Summary
There is a trend that the number of people with cardiovascular disease (CVD) is increasing year by year. Many potent synthetic ACE inhibitors have been used for the clinical treatment of hypertension in the human body [9]. These synthetic ACE inhibitors have various side effects, such as hypotension, coughing, increasing potassium level and fetal abnormalities [10]. The ACE inhibitors derived from food materials have attracted more attention [11,12]. Several ACE-inhibitory peptides from walnut proteins had been purified and identified [12,18,20]. The walnut protein hydrolysate was prepared by enzymatic digestion, and the sequence of the derived peptides was determined by UPLC-Q-TOF-MS/MS. The ACE-inhibitory kinetics of the peptide and the potential mechanism of bioactivity were proposed by using molecular docking analysis
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