Abstract
Angiotensin-I-converting enzyme (ACE) inhibitory peptides were isolated from walnut pepsin hydrolysates using ultrafiltration, Sephadex G-25 chromatography, reverse-phase high-performance liquid chromatography (RP-HPLC), and the AKTA preparative HPLC separation and purification system. ACE inhibitory activity was measured using in vitro HPLC analysis, and N-terminal amino acid sequencing was used for structural identification. Those fractions with the highest ACE inhibitory activity were further purified using RP-HPLC and the AKTA systems. The most active ACE inhibitory peptide had the sequence Tyr-Val-Pro-His-Trp-Asp-Leu and a molecular weight of 929 Da. Its activity, along with the activity of a synthetic ACE inhibitory peptide with the same sequence, was measured using HPLC following in vitro gastrointestinal digestion experiments. The IC50 values obtained before and after digestion were 0.136 and 0.173 μM/mL, respectively, which indicated that the peptide was relative stable during digestion and might have in vivo biological activity.
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