Identification of barley-derived peptides with angiotensin converting enzyme inhibitory activity
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Kaito Endo
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Takefumi Karashima
Abstract
This study aimed to obtain angiotensin converting enzyme (ACE) inhibitory peptides from barley hordein, a protein rich in proline and glutamine, and to identify novel inhibitors. Hordein was hydrolyzed using four enzymes: pepsin, trypsin, papain, and orientase, an enzyme from Aspergillus oryzae known to cleave the C-terminal side of proline residues. The hydrolysate from orientase showed strong ACE inhibitory activity. LC-MS/MS analysis identified 35 peptides, including 23 derived from hordein and 9 known ACE inhibitors. After synthesizing 15 peptides, 7 showed significant ACE inhibition, all containing proline at the C-terminus. Notably, QQP, a new peptide, exhibited notable activity (IC50 40 μM). The results suggest that barley hordein is a valuable source of ACE inhibitory peptides, with QQP as a promising candidate.
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Research ethics: Not applicable.
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Informed consent: Not applicable.
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Author contributions: All authors have accepted responsibility for the entire content of this manuscript and approved its submission. KE: Writing – review & editing, Validation, Methodology, Investigation, Formal analysis. HA: Writing – review & editing, Supervision. KK: Writing – review & editing, Methodology, Investigation, EM-S: Writing – review & editing, Methodology, Investigation, Supervision, TK: Writing – review & editing, Investigation, YK: Writing – review & editing, Investigation, HT: Writing – review & editing, Supervision, Project administration, KS: Writing – review & editing, Supervision. HH: Writing – review & editing, Writing – original draft, Supervision, Project administration, Funding acquisition.
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Use of Large Language Models, AI and Machine Learning Tools: None declared.
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Conflict of interest: This research was supported in part by Sanwa Shurui Co. Ltd. to HH. TK, YK and HT are employees of Sanwa Shurui Co Ltd. All other authors state no conflict of interest.
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Research funding: This research was supported in part by Sanwa Shurui Co. Ltd. to HH and JSPS KAKENHI (Grant Number JP22H00273) to HH, KS, and HA.
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Data availability: Not applicable.
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Supplementary Material
This article contains supplementary material (https://doi.org/10.1515/ijfe-2024-0255).
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Articles in the same Issue
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- Identification of barley-derived peptides with angiotensin converting enzyme inhibitory activity
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Articles in the same Issue
- Frontmatter
- Articles
- Cellulose particles filled oil-in-water emulsion: a facile strategy to prepare edible oleogels
- Identification of barley-derived peptides with angiotensin converting enzyme inhibitory activity
- Multiphysics simulation for microwave-assisted continuous flow in a tube flow reactor with a mode stirrer
- Regulation of Pleurotus geesteranus protein particle characteristics on the microstructure and rheology of their W1/O/W2 double emulsions
- Effect of soybean protein isolate, transglutaminase, and konjac glucomannan on the cooking and eating quality and digestibility of rice noodles
- Effect of different protease on the hydrolysis degree and antigenicity of cow milk protein
