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 ÄKTA 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 ÄKTA 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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Acknowledgments
This work was supported by the “Fundamental Research Funds for the Central University (No. TD2012-03) (No. 2015ZCQ-SW-04)” and the “Beijing Agricultural Technology Project (No. 20130110).” The authors would like to thank Hebei Jingpin Fruit Industry Company for providing the walnut meal and the Beijing Xinongsheng Biotechnology Co., Ltd. for the work on the separation using the ÄKTA system.
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Wang, FJ., Yin, XY., Regenstein, J.M. et al. Separation and purification of angiotensin-I-converting enzyme (ACE) inhibitory peptides from walnuts (Juglans regia L.) meal. Eur Food Res Technol 242, 911–918 (2016). https://doi.org/10.1007/s00217-015-2597-5
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DOI: https://doi.org/10.1007/s00217-015-2597-5